English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Comparative X-ray analysis of the unliganded fosfomycin-target MurA

Eschenburg, S., & Schönbrunn, E. (2000). Comparative X-ray analysis of the unliganded fosfomycin-target MurA. Proteins: Structure, Function, and Bioinformatics, 40(2), 290-298. doi:10.1002/(SICI)1097-0134(20000801)40:2<290:AID-PROT90>3.0.CO;2-0.

Item is

Basic

show hide
Genre: Journal Article
Alternative Title : Comparative X-ray analysis of the unliganded fosfomycin-target MurA

Files

show Files
hide Files
:
ProtStructFunctGenet_40_2000_290.pdf (Any fulltext), 612KB
 
File Permalink:
-
Name:
ProtStructFunctGenet_40_2000_290.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Creators

show
hide
 Creators:
Eschenburg, Susanne1, Author              
Schönbrunn, Ernst, Author
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

Content

show
hide
Free keywords: -
 Abstract: MurA, an essential enzyme for the synthesis of the bacterial cell wall, follows an induced-fit mechanism. Upon substrate binding, the active site forms in the interdomain cleft, involving movements of the two domains of the protein and a reorientation of the loop Pro112-Pro121. We compare two structures of un-liganded MurA from Enterobacter cloacae: a new orthorhombic form, solved to 1.80 Å resolution, and a monoclinic form, redetermined to 1.55 Å resolution. In the monoclinic form, the loop Pro112-Pro121 stretches into solvent, while in the new form it adopts a winded conformation, thereby reducing solvent accessibility of the critical residue Cys115. In the interdomain cleft a network of 27 common water molecules has been identified, which partially shields negative charges in the cleft and stabilizes the orientation of catalytically crucial residues. This could support substrate binding and ease domain movements. Near the hinge region an isoaspartyl residue has been recognized, which is the product of post-translational modification of the genetically encoded Asn67-Gly68. The homogenous population with L-isoaspartate in both structures suggests that the modification in Enterobacter cloacae MurA is not a mere aging defect but rather the result of a specific in vivo process.

Details

show
hide
Language(s): eng - English
 Dates: 1999-12-142000-03-142000-05-242000-05-24
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: bacterial cell wall; induced-fit mechanism; solvent network; deamidation; isoaspartate formation
 Rev. Type: Peer
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Proteins: Structure, Function, and Bioinformatics
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: New York, NY : John Wiley & Sons
Pages: - Volume / Issue: 40 (2) Sequence Number: - Start / End Page: 290 - 298 Identifier: ISSN: 0887-3585
CoNE: https://pure.mpg.de/cone/journals/resource/954925553393_1