Journal Issue - Volume 7 Issue 3 (March 1998)
Mechanism and evolution of protein dimerization
- Ruth Nussinov, Dong Xu, Chung‐Jung Tsai
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070301 (p 533-544)
Abstract We have investigated the mechanism and the evolutionary pathway of protein dimerization through analysis of experimental structures of dimers. We propose that the evolution of dimers may have multiple pathways, including (1) formation of a functional dimer directly without going through an ancestor monomer, (2) formation of a stable monomer as an intermediate followed by mutations of its surface residues, and (3), a domain...
Subunit asymmetry in the three‐dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis
- David Eisenberg, P. John Hart, Hongbin Liu, Matteo Pellegrini, Aram M. Nersissian, Edith B. Gralla, Joan S. Valentine
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070302 (p 545-555)
Abstract The X‐ray crystal structure of a human copper/zinc superoxide dismutase mutant (G37R CuZnSOD) found in some patients with the inherited form of Lou Gehrig's disease (FALS) has been determined to 1.9 Å resolution. The two SOD subunits have distinct environments in the crystal and are different in structure at their copper binding sites. One subunit (subunitintact) shows a four‐coordinate ligand geometry of the copper ion, whereas the...
Structures of murine carbonic anhydrase IV and human carbonic anhydrase II complexed with brinzolamide: Molecular basis of isozyme‐drug discrimination
- Travis Stams, Yun Chen, David W. Christianson, P. Ann Boriack‐Sjodin, Jonathan D. Hurt, Philip Laipis, David N. Silverman, John Liao, Jesse A. May, Tom Dean
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070303 (p 556-563)
Abstract Carbonic anhydrase IV (CAIV) is a membrane‐associated enzyme anchored to plasma membrane surfaces by a phosphatidylinositol glycan linkage. We have determined the 2.8‐Å resolution crystal structure of a truncated, soluble form of recombinant murine CAIV. We have also determined the structure of its complex with a drug used for glaucoma therapy, the sulfonamide inhibitor brinzolamide (Azopt™). The overall structure of murine...
Crystal structures of the psychrophilic α‐amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor
- Nushin Aghajari, Richard Haser, Georges Feller, Charles Gerday
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070304 (p 564-572)
Abstract Alteromonas haloplanctis is a bacterium that flourishes in Antarctic sea‐water and it is considered as an extreme psychrophile. We have determined the crystal structures of the α‐amylase (AHA) secreted by this bacterium, in its native state to 2.0 Å resolution as well as in complex with Tris to 1.85 Å resolution. The structure of AHA, which is the first experimentally determined three‐dimensional structure of a...
Solvation studies of DMP323 and A76928 bound to HIV protease: Analysis of water sites using grand canonical Monte Carlo simulations
- Tami J. Marrone, J. Andrew McCammon, Haluk Resat, C. Nicholas Hodge, Chong‐Hwan Chang
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070305 (p 573-579)
Abstract We examine the water solvation of the complex of the inhibitors DMP323 and A76928 bound to HIV‐1 protease through grand canonical Monte Carlo simulations, and demonstrate the ability of this method to reproduce crystal waters and effectively predict water positions not seen in the DMP323 or A76928 structures. The simulation method is useful for identifying structurally important waters that may not be resolved in the...
Crystallization of phycoerythrin 545 of Rhodomonas lens using detergents and unusual additives
- Michael Becker, Milton T. Stubbs, Robert Huber
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070306 (p 580-586)
Abstract Phycoerythrin 545 from the cryptomonad alga, Rhodomonas lens, has been crystallized under a wide variety of conditions. Although this type of photosynthetic light‐harvesting protein is water soluble, detergents were always required for crystallization. The crystals were typically poorly ordered, or ordered in only two dimensions. However, crystals that were well‐ordered in three dimensions could be obtained under two different ...
A proposed architecture for lecithin cholesterol acyl transferase (LCAT): Identification of the catalytic triad and molecular modeling
- F. Peelman, N. Vinaimont, B. Vanloo, C. Labeur, M. Rosseneu, A. Verhee, J‐L. Verschelde, J. Vanderckove, J. Tavernier, S. Seguret‐Mace, N. Duverger, G. Hutchinson
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070307 (p 587-599)
Abstract The enzyme cholesterol lecithin acyl transferase (LCAT) shares the Ser/Asp‐Glu/His triad with lipases, esterases and proteases, but the low level of sequence homology between LCAT and these enzymes did not allow for the LCAT fold to be identified yet. We, therefore, relied upon structural homology calculations using threading methods based on alignment of the sequence against a library of solved three‐dimensional protein...
Cadmium‐induced crystallization of proteins: II. Crystallization of the Salmonella typhimuri histidine‐binding protein in complex with L‐histidine, L‐arginine, or L‐lysine
- Giovanna Ferro‐Luzzi Ames, David I. Kreimer, Sergei Trakhanov, Sean Parkin, Bernhard Rupp
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070308 (p 600-604)
Abstract To further investigate favorable effects of divalent cations on the formation of protein crystals, three complexes of Salmonella typhimurium histidine‐binding protein were crystallized with varying concentrations of cadmium salts. For each of the three histidine‐binding protein complexes, cadmium cations were found to promote or improve crystallization. The optimal cadmium concentration is ligand specific and falls within a narrow...
Comparisons between the structures of HCV and Rep helicases reveal structural similarities between SF1 and SF2 super‐families of helicases
- Sergey Korolev, Timothy M. Lohman, Gabriel Waksman, Nanhua Yao, Patricia C. Weber
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070309 (p 605-610)
Abstract Three helicase structures have been determined recently: that of the DNA helicase PcrA, that of the hepatitis C virus RNA helicase, and that of the Escherichia coli DNA helicase Rep. PcrA and Rep belong to the same super‐family of helicases (SF1) and are structurally very similar. In contrast, the HCV helicase belongs to a different super‐family of helicases, SF2, and shows little sequence homology with the PcrA/Rep ...
X‐ray structures of three interface mutants of γB‐crystallin from bovine eye lens
- Stefan Palme, Christine Slingsby, Rainer Jaenicke
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070310 (p 611-618)
Abstract γB‐crystallin consists of two domains each comprising two “Greek key” motifs. Both domains fold independently, and domain interactions contribute significantly to the stability of the C‐terminal domain. In a previous study (Palme S et al., 1996, Protein Sci 6:1529‐1636) it was shown that Phe56 from the N‐terminal domain, a residue involved in forming a hydrophobic core at the domain interface, effects the interaction of the...
Solution structure of Compstatin, a potent complement inhibitor
- Dimitrios Morikis, Nuria Assa‐Munt, Arvind Sahu, John D. Lambris
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070311 (p 619-627)
Abstract The third component of complement, C3, plays a central role in activation of the classical, alternative, and lectin pathways of complement activation. Recently, we have identified a 13‐residue cyclic peptide (named Compstatin) that specifically binds to C3 and inhibits complement activation. To investigate the topology and the contribution of each critical residue to the binding of Compstatin to C3, we have now determined...
Mutational analysis of human DNase I at the DNA binding interface: Implications for DNA recognition, catalysis, and metal ion dependence
- Clark Q. Pan, Jana S. Uumer, Andrea Herzka, Robert A. Lazarus
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070312 (p 628-636)
Abstract Human deoxyribonuclease I (DNase I), an enzyme used to treat cystic fibrosis patients, has been systematically analyzed by site‐directed mutagenesis of residues at the DNA binding interface. Crystal structures of bovine DNase I complexed with two different oligonucleotides have implicated the participation of over 20 amino acids in catalysis or DNA recognition. These residues have been classified into four groups based on...
Role of the amino‐terminal region of streptokinase in the generation of a fully functional plasminogen activator complex probed with synthetic peptides
- Deepak Nihalani, Rajesh Kumarm, K. Rajagopal, Girish Sahni
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070313 (p 637-648)
Abstract The mechanism whereby fragments of streptokinase (SK) derived from its N terminus (e.g., SK1‐59 or SK1‐63) enhance the low plasminogen (PG)‐activating ability of other fragments, namely SK64‐386, SK60‐414, SK60‐387, and SK60‐333 (reported previously), has been investigated using a synthetic peptide approach. The addition of either natural SK1‐59, or chemically synthesized SK16‐59, at saturation (about 500‐fold molar excess)...
Locally accessible conformations of proteins: Multiple molecular dynamics simulations of crambin
- Jeffrey D. Evanseck, Leo S. D. Caves, Martin Karplus
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070314 (p 649-666)
Abstract Multiple molecular dynamics (MD) simulations of crambin with different initial atomic velocities are used to sample conformations in the vicinity of the native structure. Individual trajectories of length up to 5 ns sample only a fraction of the conformational distribution generated by ten independent 120 ps trajectories at 300 K. The backbone atom conformational space distribution is analyzed using principal components...
Spider minor ampullate silk proteins contain new repetitive sequences and highly conserved non‐silk‐like “spacer regions”
- Mark A. Colgin, Randolph V. Lewis
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560070315 (p 667-672)
Abstract Spider minor ampullate silk is a strong non‐elastic deformably stretchable silk used in web formation. This silk from Nephila clavipes is composed of two proteins, MiSp 1 and 2, whose transcripts are 9.5 and 7.5 kb, respectively, as determined by northern blots. Both MiSp proteins are organized into a predominantly repetitive region and a small nonrepetitive carboxy terminal region. These highly repetitive regions are composed mainly...




