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4jxb
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4jxb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JXB FirstGlance]. <br> | <table><tr><td colspan='2'>[[4jxb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JXB FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.56Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></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=4jxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jxb OCA], [https://pdbe.org/4jxb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jxb RCSB], [https://www.ebi.ac.uk/pdbsum/4jxb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jxb ProSAT]</span></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=4jxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jxb OCA], [https://pdbe.org/4jxb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jxb RCSB], [https://www.ebi.ac.uk/pdbsum/4jxb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jxb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/O06624_MYCTU O06624_MYCTU] | [https://www.uniprot.org/uniprot/O06624_MYCTU O06624_MYCTU] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Enzymes carrying NlpC/p60 domains, for instance RipA and RipB from Mycobacterium tuberculosis, are bacterial peptidoglycan hydrolases cleaving the peptide stems and contribute to cell wall remodeling during cell division. A member of this protein family, RipD (Rv1566c) from M. tuberculosis described here, displays sequence alterations in the NlpC/p60 catalytic triad and carries a pentapeptide repeat at its carboxy-terminus. Bioinformatics analysis revealed RipD-like proteins in eleven mycobacterial genomes, while similar pentapeptide-repeats occur in cell wall-localized bacterial proteins and in a mycobacteriophage. In contrast to previously known members of the NlpC/p60 family, RipD does not show peptidoglycan hydrolase activity, which is consistent with the sequence alterations at the catalytic site. A strong interaction of the catalytically inactive core domain with peptidoglycan is however retained, presenting the first example of the NlpC/p60 domains that evolved to a non-catalytic peptidoglycan binding function. Full-length RipD, carrying the C-terminal repeat, shows however a decrease in binding affinity to peptidoglycan, suggesting that the C-terminal tail modulates the interaction with bacterial call wall components. The pentapeptide repeat at the carboxy-terminus does not adopt a defined secondary structure in solution which is in accordance with results from the 1.17A crystal structure of the protein carrying two repeat units. | ||
| - | |||
| - | RipD (Rv1566c) from Mycobacterium tuberculosis: adaptation of an NlpC/p60 domain to a non-catalytic peptidoglycan-binding function.,Both D, Steiner EM, Izumi A, Schneider G, Schnell R Biochem J. 2013 Oct 10. PMID:24107184<ref>PMID:24107184</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4jxb" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
RipD (Rv1566c) from Mycobacterium tuberculosis: a non-catalytic NlpC/p60 domain protein, adaptation to peptidoglycan-binding function
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