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4lj1

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==RipD (Rv1566c) from Mycobacterium tuberculosis: a non-catalytic NlpC/p60 domain protein with two penta-peptide repeat units (PVQQA-PVQPA)==
==RipD (Rv1566c) from Mycobacterium tuberculosis: a non-catalytic NlpC/p60 domain protein with two penta-peptide repeat units (PVQQA-PVQPA)==
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<StructureSection load='4lj1' size='340' side='right' caption='[[4lj1]], [[Resolution|resolution]] 1.17&Aring;' scene=''>
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<StructureSection load='4lj1' size='340' side='right'caption='[[4lj1]], [[Resolution|resolution]] 1.17&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4lj1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LJ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LJ1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4lj1]] is a 1 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=4LJ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LJ1 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RVBD_1566c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.17&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lj1 OCA], [http://pdbe.org/4lj1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lj1 RCSB], [http://www.ebi.ac.uk/pdbsum/4lj1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lj1 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4lj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lj1 OCA], [https://pdbe.org/4lj1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lj1 RCSB], [https://www.ebi.ac.uk/pdbsum/4lj1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lj1 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/O06624_MYCTU O06624_MYCTU]
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4lj1" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Myctu]]
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[[Category: Large Structures]]
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[[Category: Both, D]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Linder, D C]]
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[[Category: Both D]]
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[[Category: Schneider, G]]
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[[Category: Linder DC]]
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[[Category: Schnell, R]]
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[[Category: Schneider G]]
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[[Category: Steiner, E M]]
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[[Category: Schnell R]]
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[[Category: Cell invasion]]
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[[Category: Steiner EM]]
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[[Category: Cell wall stabilisation]]
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[[Category: Nlpc/p60]]
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[[Category: Periplasmic]]
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Current revision

RipD (Rv1566c) from Mycobacterium tuberculosis: a non-catalytic NlpC/p60 domain protein with two penta-peptide repeat units (PVQQA-PVQPA)

PDB ID 4lj1

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