Journal Issue - Volume 18 Issue 7 (July 2009)
Probing the conformation of the resting state of a bacterial multidrug ABC transporter, BmrA, by a site‐directed spin labeling approach
- Marie‐Ange Do Cao, Serge Crouzy, Miyeon Kim, Michel Becchi, David S. Cafiso, Attilio Di Pietro, Jean‐Michel Jault
- Published in Wiley Interscience on Apr 16, 2009
- DOI: 10.1002/pro.141 (p 1507-1520)
Abstract Previously published 3‐D structures of a prototypic ATP‐binding cassette (ABC) transporter, MsbA, have been recently corrected revealing large rigid‐body motions possibly linked to its catalytic cycle. Here, a closely related multidrug bacterial ABC transporter, BmrA, was studied using site‐directed spin labeling by focusing on a region connecting the transmembrane domain and the nucleotide‐binding domain (NBD). Electron...
Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process
- Jed J. W. Wiltzius, Stuart A. Sievers, Michael R. Sawaya, David Eisenberg
- Published in Wiley Interscience on Apr 29, 2009
- DOI: 10.1002/pro.145 (p 1521-1530)
Abstract Islet Amyloid Polypeptide (IAPP or amylin) is a peptide hormone produced and stored in the β‐islet cells of the pancreas along with insulin. IAPP readily forms amyloid fibrils in vitro, and the deposition of fibrillar IAPP has been correlated with the pathology of type II diabetes. The mechanism of the conversion that IAPP undergoes from soluble to fibrillar forms has been unclear. By chaperoning IAPP through fusion to maltose binding ...
Charge neutralization and collapse of the C‐terminal tail of alpha‐synuclein at low pH
- Sebastian McClendon, Carla C. Rospigliosi, David Eliezer
- Published in Wiley Interscience on Apr 29, 2009
- DOI: 10.1002/pro.149 (p 1531-1540)
Abstract Alpha‐synuclein (αS) is the primary component of Lewy bodies, the pathological hallmark of Parkinson's Disease. Aggregation of αS is thought to proceed from a primarily disordered state with nascent secondary structure through intermediate conformations to oligomeric forms and finally to mature amyloid fibrils. Low pH conditions lead to conformational changes associated with increased αS fibril formation. Here we...
Insight into a strategy for attenuating AmpC‐mediated β‐lactam resistance: Structural basis for selective inhibition of the glycoside hydrolase NagZ
- Misty D. Balcewich, Keith A. Stubbs, Yuan He, Terrence W. James, Gideon J. Davies, David J. Vocadlo, Brian L. Mark
- Published in Wiley Interscience on Apr 16, 2009
- DOI: 10.1002/pro.137 (p 1541-1551)
Abstract NagZ is an exo‐N‐acetyl‐β‐glucosaminidase, found within Gram‐negative bacteria, that acts in the peptidoglycan recycling pathway to cleave N‐acetylglucosamine residues off peptidoglycan fragments. This activity is required for resistance to cephalosporins mediated by inducible AmpC β‐lactamase. NagZ uses a catalytic mechanism involving a covalent glycosyl enzyme intermediate, unlike that of the human...
Mutations of key hydrophobic surface residues of 11β‐hydroxysteroid dehydrogenase type 1 increase solubility and monodispersity in a bacterial expression system
- Alexander J. Lawson, Elizabeth A. Walker, Scott A. White, Timothy R. Dafforn, Paul M. Stewart, Jonathan P. Ride
- Published in Wiley Interscience on Apr 29, 2009
- DOI: 10.1002/pro.150 (p 1552-1563)
Abstract 11β‐Hydroxysteroid dehydrogenase type 1 (11β‐HSD1) is a key enzyme in the conversion of cortisone to the functional glucocorticoid hormone cortisol. This activation has been implicated in several human disorders, notably the metabolic syndrome where 11β‐HSD1 has been identified as a novel target for potential therapeutic drugs. Recent crystal structures have revealed the presence of a pronounced hydrophobic surface patch...
Mistic: Cellular localization, solution behavior, polymerization, and fibril formation
- Hay Dvir, Matthew E. Lundberg, Samir K. Maji, Roland Riek, Senyon Choe
- Published in Wiley Interscience on Apr 29, 2009
- DOI: 10.1002/pro.148 (p 1564-1570)
Abstract Mistic represents a family of unique membrane‐associating proteins originally found in Bacillus subtilis (M110). As a fusion partner, it has been shown to assist overexpression of foreign integral membrane proteins in E. coli. We have expressed shorter Mistic homologs from other Bacillus species and surprisingly, unlike M110, found them abundant in the cytoplasm. These Mistic homologs including the corresponding shorter sequence (amino acids 27...
Nanoscale elongating control of the self‐assembled protein filament with the cysteine‐introduced building blocks
- Kengo Usui, Tei Maki, Fuyu Ito, Atsushi Suenaga, Satoru Kidoaki, Masayoshi Itoh, Makoto Taiji, Takehisa Matsuda, Yoshihide Hayashizaki, Harukazu Suzuki
- Published in Wiley Interscience on May 20, 2009
- DOI: 10.1002/pro.161 (p 1571-1571)




