3slu: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3slu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SLU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SLU FirstGlance]. <br>
<table><tr><td colspan='2'>[[3slu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SLU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SLU FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene><br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HMPREF0602_0018 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=487 Neisseria meningitidis])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HMPREF0602_0018 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=487 Neisseria meningitidis])</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3slu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3slu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3slu RCSB], [http://www.ebi.ac.uk/pdbsum/3slu PDBsum]</span></td></tr>
<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=3slu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3slu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3slu RCSB], [http://www.ebi.ac.uk/pdbsum/3slu PDBsum]</span></td></tr>
<table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Neisseria meningitidis]]
[[Category: Neisseria meningitidis]]
[[Category: Shen, Y.]]
[[Category: Shen, Y]]
[[Category: Wang, X.]]
[[Category: Wang, X]]
[[Category: Xu, H.]]
[[Category: Xu, H]]
[[Category: Yang, X.]]
[[Category: Yang, X]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Outer membrane]]
[[Category: Outer membrane]]

Revision as of 12:54, 4 January 2015

Crystal structure of NMB0315Crystal structure of NMB0315

Structural highlights

3slu is a 2 chain structure with sequence from Neisseria meningitidis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:HMPREF0602_0018 (Neisseria meningitidis)
Resources:FirstGlance, OCA, RCSB, PDBsum

Publication Abstract from PubMed

NMB0315 is an outer membrane protein of Neisseria meningitidis serogroup B (NMB) and a potential candidate for a broad-spectrum vaccine against meningococcal disease. The crystal structure of NMB0315 was solved by single-wavelength anomalous dispersion (SAD) at a resolution of 2.4 A and revealed to be a lysostaphin-type peptidase of the M23 metallopeptidase family. The overall structure consists of three well-separated domains and has no similarity to any previously published structure. However, only the topology of the carboxyl-terminal domain is highly conserved among members of this family, and this domain is a zinc-dependent catalytic unit. The amino-terminal domain of the structure blocks the substrate binding pocket in the carboxyl-terminal domain, indicating that the wild-type full-length protein is in an inactive conformational state. Our studies improve the understanding of the catalytic mechanism of M23 metallopeptidases.

Crystal structure of outer membrane protein NMB0315 from Neisseria meningitidis.,Wang X, Yang X, Yang C, Wu Z, Xu H, Shen Y PLoS One. 2011;6(10):e26845. Epub 2011 Oct 26. PMID:22046377[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Wang X, Yang X, Yang C, Wu Z, Xu H, Shen Y. Crystal structure of outer membrane protein NMB0315 from Neisseria meningitidis. PLoS One. 2011;6(10):e26845. Epub 2011 Oct 26. PMID:22046377 doi:10.1371/journal.pone.0026845

3slu, resolution 2.41Å

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OCA