8aud: Difference between revisions
New page: '''Unreleased structure''' The entry 8aud is ON HOLD Authors: Description: Category: Unreleased Structures |
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The | ==Structure of peptidoglycan hydrolase Cg1735 from Corynebacterium glutamicum, orthorhombic crystal form== | ||
<StructureSection load='8aud' size='340' side='right'caption='[[8aud]], [[Resolution|resolution]] 4.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8aud]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum_ATCC_13032 Corynebacterium glutamicum ATCC 13032]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AUD FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.5Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8aud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aud OCA], [https://pdbe.org/8aud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aud RCSB], [https://www.ebi.ac.uk/pdbsum/8aud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aud ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8NQA0_CORGL Q8NQA0_CORGL] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The bacterial cell wall is a multi-layered mesh, whose major component is peptidoglycan (PG), a sugar polymer cross-linked by short peptide stems. During cell division, a careful balance of PG synthesis and degradation, precisely coordinated both in time and space, is necessary to prevent uncontrolled destruction of the cell wall. In Corynebacteriales, the D,L endopeptidase RipA has emerged as a major PG hydrolase for cell separation, and RipA defaults have major implications for virulence of the human pathogens Mycobacterium tuberculosis and Corynebacterium diphtheriae. However, the precise mechanisms by which RipA mediates cell separation remain elusive. Here we report phylogenetic, biochemical, and structural analysis of the Corynebacterium glutamicum homologue of RipA, Cg1735. The crystal structures of full-length Cg1735 in two different crystal forms revealed the C-terminal NlpC/P60 catalytic domain obtruded by its N-terminal conserved coiled-coil domain, which locks the enzyme in an autoinhibited state. We show that this autoinhibition is relieved by the extracellular core domain of the transmembrane septal protein Cg1604. The crystal structure of Cg1604 revealed a (beta/alpha) protein with an overall topology similar to that of receiver domains from response regulator proteins. The atomic model of the Cg1735-Cg1604 complex, based on bioinformatical and mutational analysis, indicates that a conserved, distal-membrane helical insertion in Cg1604 is responsible for Cg1735 activation. The reported data provide important insights into how intracellular cell division signal(s), yet to be identified, control PG hydrolysis during RipA-mediated cell separation in Corynebacteriales. | |||
FtsEX-independent control of RipA-mediated cell separation in Corynebacteriales.,Gaday Q, Megrian D, Carloni G, Martinez M, Sokolova B, Ben Assaya M, Legrand P, Brule S, Haouz A, Wehenkel AM, Alzari PM Proc Natl Acad Sci U S A. 2022 Dec 13;119(50):e2214599119. doi: , 10.1073/pnas.2214599119. Epub 2022 Dec 5. PMID:36469781<ref>PMID:36469781</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8aud" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Corynebacterium glutamicum ATCC 13032]] | |||
[[Category: Large Structures]] | |||
[[Category: Alzari PM]] | |||
[[Category: Gaday Q]] | |||
[[Category: Wehenkel AM]] | |||
Latest revision as of 16:38, 1 February 2024
Structure of peptidoglycan hydrolase Cg1735 from Corynebacterium glutamicum, orthorhombic crystal formStructure of peptidoglycan hydrolase Cg1735 from Corynebacterium glutamicum, orthorhombic crystal form
Structural highlights
FunctionPublication Abstract from PubMedThe bacterial cell wall is a multi-layered mesh, whose major component is peptidoglycan (PG), a sugar polymer cross-linked by short peptide stems. During cell division, a careful balance of PG synthesis and degradation, precisely coordinated both in time and space, is necessary to prevent uncontrolled destruction of the cell wall. In Corynebacteriales, the D,L endopeptidase RipA has emerged as a major PG hydrolase for cell separation, and RipA defaults have major implications for virulence of the human pathogens Mycobacterium tuberculosis and Corynebacterium diphtheriae. However, the precise mechanisms by which RipA mediates cell separation remain elusive. Here we report phylogenetic, biochemical, and structural analysis of the Corynebacterium glutamicum homologue of RipA, Cg1735. The crystal structures of full-length Cg1735 in two different crystal forms revealed the C-terminal NlpC/P60 catalytic domain obtruded by its N-terminal conserved coiled-coil domain, which locks the enzyme in an autoinhibited state. We show that this autoinhibition is relieved by the extracellular core domain of the transmembrane septal protein Cg1604. The crystal structure of Cg1604 revealed a (beta/alpha) protein with an overall topology similar to that of receiver domains from response regulator proteins. The atomic model of the Cg1735-Cg1604 complex, based on bioinformatical and mutational analysis, indicates that a conserved, distal-membrane helical insertion in Cg1604 is responsible for Cg1735 activation. The reported data provide important insights into how intracellular cell division signal(s), yet to be identified, control PG hydrolysis during RipA-mediated cell separation in Corynebacteriales. FtsEX-independent control of RipA-mediated cell separation in Corynebacteriales.,Gaday Q, Megrian D, Carloni G, Martinez M, Sokolova B, Ben Assaya M, Legrand P, Brule S, Haouz A, Wehenkel AM, Alzari PM Proc Natl Acad Sci U S A. 2022 Dec 13;119(50):e2214599119. doi: , 10.1073/pnas.2214599119. Epub 2022 Dec 5. PMID:36469781[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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