Journal Issue - Volume 8 Issue 3 (1999)
Structure and dynamics in solution of the complex of lactobacillus casei dihydrofolate reductase with the new lipophilic antifolate drug trimetrexate
- Vladimir I. Polshakov, Berry Birdsall, Thomas A. Frenkiel, Angelo R. Gargaro, James Feeney
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.8.3.467 (p 467-481)
Abstract We have determined the three‐dimensional solution structure of the complex of Lactobacillus casei dihydrofolate reductase and the anticancer drug trimetrexate. Two thousand seventy distance, 345 dihedral angle, and 144 hydrogen bond restraints were obtained from analysis of multidimensional NMR spectra recorded for complexes containing 15N‐labeled protein. Simulated annealing calculations produced a family of 22 structures fully consistent with...
Solution assembly of the pseudo‐high affinity and intermediate affinity interleukin‐2 receptor complexes
- Zining Wu, Byron Goldstein, Thomas M. Laue, Stefano F. Liparoto, Michael J. Nemeth, Thomas L. Ciardelli
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.8.3.482 (p 482-489)
Abstract The high affinity interleukin‐2 receptor is composed of three cell surface subunits, IL‐2Rα, IL‐2Rβ, and IL‐2Rγ. Functional forms of the IL‐2 receptor exist, however, that enlist only two of the three subunits. On activated T‐cells, the α‐ and β‐subunits combine as a preformed heterodimer (the pseudo‐high affinity receptor) that serves to capture IL‐2. On a subpopulation of natural killer cells, the β‐ and γ‐subunits...
Role of the lateral channel in catalase HPII of Escherichia coli
- M. Serdal Sevinc, Maria J. Maté, Jack Switala, Ignacio Fita, Peter C. Loewen
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.8.3.490 (p 490-498)
Abstract The heme‐containing catalase HPII of Escherichia coli consists of a homotetramer in which each subunit contains a core region with the highly conserved catalase tertiary structure, to which are appended N‐ and C‐terminal extensions making it the largest known catalase. HPII does not bind NADPH, a cofactor often found in catalases. In HPII, residues 585–590 of the C‐terminal extension protrude into the pocket corresponding to ...
The solution structure of a superpotent b‐chain‐shortened single‐replacement insulin analogue
- Günther Kurapkat, Michael Siedentop, Hans‐Gregor Gattner, Michael Hagelstein, Dietrich Brandenburg, Joachim Grötzinger, Axel Wollmer
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.8.3.499 (p 499-508)
Abstract This paper reports on an insulin analogue with 12.5‐fold receptor affinity, the highest increase observed for a single replacement, and on its solution structure, determined by NMR spectroscopy. The analogue is [D‐AlaB26]des‐(B27‐B30)‐tetrapeptide‐insulin‐B26‐amide. C‐terminal truncation of the B‐chain by four (or five) residues is known not to affect the functional properties of insulin, provided the...
Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains
- Rosemarie Raffen, Lynda J. Dieckman, Meredith Szpunar, Christine Wunschl, Phani R. Pokkuluri, Poras Dave, Priscilla Wilkins Stevens, Xiaoyin Cai, Marianne Schiffer, Fred J. Stevens
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.8.3.509 (p 509-517)
Abstract The most common form of systemic amyloidosis originates from antibody light chains. The large number of amino acid variations that distinguish amyloidogenic from nonamyloidogenic light chain proteins has impeded our understanding of the structural basis of light‐chain fibril formation. Moreover, even among the subset of human light chains that are amyloidogenic, many primary structure differences are found. We compared the...
Mapping cyclic nucleotide‐induced conformational changes in cyclicAMP receptor protein by a protein footprinting technique using different chemical proteases
- Noel Baichoo, Tomasz Heyduk
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.8.3.518 (p 518-528)
Abstract CyclicAMP receptor protein (CRP) regulates transcription of numerous genes in Escherichia coli. Both cAMP and cGMP bind CRP, but only cAMP induces conformational changes that dramatically increase the specific DNA binding activity of the protein. We have shown previously that our protein footprinting technique is sensitive enough to detect conformational changes in CRP by cAMP [Baichoo N, Heyduk T. 1997. Biochemistry 36:10830–10836]....
Domain exchange experiments in duck d‐crystallins: Functional and evolutionary implications
- Liliana M. Sampaleanu, Alan R. Davidson, Caroline Graham, Graeme J. Wistow, P. Lynne Howell
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.8.3.529 (p 529-537)
Abstract δ‐Crystallin, the major soluble protein component of the avian and reptilian eye lens, is homologous to the urea cycle enzyme argininosuccinate lyase (ASL). In duck lenses there are two δ crystallins, denoted δ1 and δ2. Duck δ2 is both a major structural protein of the lens and also the duck orthologue of ASL, an example of gene recruitment. Although 94% identical to δ2/ASL in the amino acid sequence, δ1 is enzymatically...
Crystal structure of thymidylate synthase A from Bacillus subtilis
- Kristin M. Fox, Frank Maley, Araik Garibian, Li‐Ming Changchien, Patrick Van Roey
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.8.3.538 (p 538-544)
Abstract Thymidylate synthase (TS) converts dUMP to dTMP by reductive methylation, where 5,10‐methylenetetrahydrofolate is the source of both the methylene group and reducing equivalents. The mechanism of this reaction has been extensively studied, mainly using the enzyme from Escherichia coli. Bacillus subtilis contains two genes for TSs, ThyA and ThyB. The ThyB enzyme is very similar to other bacterial TSs, but the ThyA enzyme is ...
Two well‐defined motifs in the cAMP‐dependent protein kinase inhibitor (PKIα) correlate with inhibitory and nuclear export function
- Jennifer A. Hauer, Philippe Barthe, Susan S. Taylor, Joseph Parello, André Padilla
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.8.3.545 (p 545-553)
Abstract The heat stable inhibitor of cAMP‐dependent protein kinase (PKIα) contains both a nuclear export signal (NES) and a high affinity inhibitory region that is essential for inhibition of the catalytic subunit of the kinase. These functions are sequentially independent. Two‐dimensional NMR spectroscopy was performed on uniformly [15N]‐labeled PKIα to examine its structure free in solution. Seventy out of 75 residues were identified, and...
Energetics of solvent and ligand‐induced conformational changes in α‐lactalbumin
- Yuri V. Griko, David P. Remeta
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.8.3.554 (p 554-561)
Abstract The energetics of structural changes in the holo and apo forms of α‐lactalbumin and the transition between their native and denatured states induced by binding Ca2+ and Na+ have been studied by differential scanning and isothermal titration microcalorimetry and circular dichroism spectroscopy under various solvent conditions. Removal of Ca2+ from the protein enhances its sensitivity to pH and ionic conditions due to noncompensated...
Structure in the channel forming domain of colicin E1 bound to membranes: The 402–424 sequence
- Ukasz SalwiSki, Wayne L. Hubbell
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.8.3.562 (p 562-572)
Abstract To explore the structure of the pore‐forming fragment of colicin E1 in membranes, a series of 23 consecutive single cysteine substitution mutants was prepared in the sequence 402–424. Each mutant was reacted with a sulfhydryl‐specific reagent to generate a nitroxide labeled side chain, and the mobility of the side chain and its accessibility to collision with paramagnetic reagents was determined from the electron...
Analysis of interactive packing of secondary structural elements in α/β units in proteins
- Boojala V.B. Reddy, Hampapathalu A. Nagarajaram, Tom L. Blundell
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.8.3.573 (p 573-586)
Abstract An α‐helix and a β‐strand are said to be interactively packed if at least one residue in each of the secondary structural elements loses 10% of its solvent accessible contact area on association with the other secondary structural element.An analysis of all such 5,975 nonidentical α/β units in protein structures, defined at 2.5Å resolution, shows that the interaxial distance between the α‐helix and theβ‐strand is linearly...
A survey of left‐handed polyproline II helices
- Benjamin J. Stapley, Trevor P. Creamer
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.8.3.587 (p 587-595)
Abstract Left‐handed polyproline II helices (PPII) are contiguous elements of protein secondary structure in which the ø and Ψ angles of constituent residues are restricted to around –75° and 145°, respectively. They are important in structural proteins, in unfolded states and as ligands for signaling proteins. Here, we present a survey of 274 nonhomologous polypeptide chains from proteins of known structure for regions that form...
The mechanism of sugar phosphate isomerization by glucosamine 6‐phosphate synthase
- Alexei Teplyakov, Galya Obmolova, Marie‐Ange Badet‐Denisot, Bernard Badet
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.8.3.596 (p 596-602)
Abstract Glucosamine 6‐phosphate synthase converts fructose‐6P into glucosamine‐6P or glucose‐6P depending on the presence or absence of glutamine. The isomerase activity is associated with a 40‐kDa C‐terminal domain, which has already been characterized crystallographically. Now the three‐dimensional structures of the complexes with the reaction product glucose‐6P and with the transition state analog 2‐amino‐2‐deoxyglucitol‐6P have...
Comparison of protein–protein interactions in serine protease‐inhibitor and antibody‐antigen complexes: Implications for the protein docking problem
- Richard M. Jackson
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.8.3.603 (p 603-613)
Abstract The protein‐protein interaction energy of 12 nonhomologous serine protease‐inhibitor and 15 antibody‐antigen complexes is calculated using a molecular mechanics formalism and dissected in terms of the main‐chain vs. side‐chain contribution, nonrotameric side‐chain contributions, and amino acid residue type involvement in the interface interaction. There are major differences in the interactions of the...




