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| - | [[Image:1crz.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1crz| PDB=1crz | SCENE= }} | | {{STRUCTURE_1crz| PDB=1crz | SCENE= }} |
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| - | '''CRYSTAL STRUCTURE OF THE E. COLI TOLB PROTEIN'''
| + | ===CRYSTAL STRUCTURE OF THE E. COLI TOLB PROTEIN=== |
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| - | ==Overview==
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| - | BACKGROUND: The periplasmic protein TolB from Escherichia coli is part of the Tol-PAL (peptidoglycan-associated lipoprotein) multiprotein complex used by group A colicins to penetrate and kill cells. TolB homologues are found in many gram-negative bacteria and the Tol-PAL system is thought to play a role in bacterial envelope integrity. TolB is required for lethal infection by Salmonella typhimurium in mice. RESULTS: The crystal structure of the selenomethionine-substituted TolB protein from E. coli was solved using multiwavelength anomalous dispersion methods and refined to 1. 95 A. TolB has a two-domain structure. The N-terminal domain consists of two alpha helices, a five-stranded beta-sheet floor and a long loop at the back of this floor. The C-terminal domain is a six-bladed beta propeller. The small, possibly mobile, contact area (430 A(2)) between the two domains involves residues from the two helices and the first and sixth blades of the beta propeller. All available genomic sequences were used to identify new TolB homologues in gram-negative bacteria. The TolB structure was then interpreted using the observed conservation pattern. CONCLUSIONS: The TolB beta-propeller C-terminal domain exhibits sequence similarities to numerous members of the prolyl oligopeptidase family and, to a lesser extent, to class B metallo-beta-lactamases. The alpha/beta N-terminal domain shares a structural similarity with the C-terminal domain of transfer RNA ligases. We suggest that the TolB protein might be part of a multiprotein complex involved in the recycling of peptidoglycan or in its covalent linking with lipoproteins.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10545334}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10545334 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10545334}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Rigal, A.]] | | [[Category: Rigal, A.]] |
| | [[Category: Two domains: beta propeller and alpha/beta fold]] | | [[Category: Two domains: beta propeller and alpha/beta fold]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:03:10 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:14:58 2008'' |
Revision as of 18:15, 30 June 2008
Template:STRUCTURE 1crz
CRYSTAL STRUCTURE OF THE E. COLI TOLB PROTEIN
Template:ABSTRACT PUBMED 10545334
About this Structure
1CRZ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of the Escherichia coli TolB protein determined by MAD methods at 1.95 A resolution., Abergel C, Bouveret E, Claverie JM, Brown K, Rigal A, Lazdunski C, Benedetti H, Structure. 1999 Oct 15;7(10):1291-300. PMID:10545334
Page seeded by OCA on Mon Jun 30 21:14:58 2008
