3hq2: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
Line 3: Line 3:
<StructureSection load='3hq2' size='340' side='right'caption='[[3hq2]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='3hq2' size='340' side='right'caption='[[3hq2]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3hq2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HQ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HQ2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3hq2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HQ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HQ2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=F:FLUORIDE+ION'>F</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.9&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BSU22080, ypwA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=F:FLUORIDE+ION'>F</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3hq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hq2 OCA], [https://pdbe.org/3hq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hq2 RCSB], [https://www.ebi.ac.uk/pdbsum/3hq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hq2 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=3hq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hq2 OCA], [https://pdbe.org/3hq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hq2 RCSB], [https://www.ebi.ac.uk/pdbsum/3hq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hq2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CBP1_BACSU CBP1_BACSU]] Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues. Has lower activity with substrates ending with His or Trp.<ref>PMID:19544567</ref>
[https://www.uniprot.org/uniprot/CBP1_BACSU CBP1_BACSU] Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues. Has lower activity with substrates ending with His or Trp.<ref>PMID:19544567</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 20: Line 20:
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hq2 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hq2 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
M32 carboxypeptidases are a distinct family of HEXXH metalloproteases whose structures exhibit a narrow substrate groove that is blocked at one end. Structural alignments with other HEXXH metalloprotease-peptide complexes suggested an orientation in which the substrate is directed towards the back of the groove. This led us to hypothesize, and subsequently confirm that the maximum substrate length for M32 carboxypeptidases is restricted. Structural and sequence analyses implicate a highly conserved Arg at the back of the groove as being critical for this length restriction. However, the Thermus thermophilus and Bacillus subtilis M32 members lack this conserved Arg. Herein, we present the biochemical and structural characterization of these two proteins. Our findings support the important role of the conserved Arg in maintaining the length restriction, and reveal a proline-rich loop as an alternate blocking strategy. Based on our results, we propose that M32 carboxypeptidases from Bacilli belong to a separate subfamily. Proteins 2009. (c) 2009 Wiley-Liss, Inc.
Insight into the substrate length restriction of M32 carboxypeptidases: Characterization of two distinct subfamilies.,Lee MM, Isaza CE, White JD, Chen RP, Liang GF, He HT, Chan SI, Chan MK Proteins. 2009 May 11;77(3):647-657. PMID:19544567<ref>PMID:19544567</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3hq2" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
Line 36: Line 27:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Vibrio subtilis ehrenberg 1835]]
[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chan, M K]]
[[Category: Chan MK]]
[[Category: Chan, S I]]
[[Category: Chan SI]]
[[Category: Chen, R P.Y]]
[[Category: Chen RP-Y]]
[[Category: He, H T.F]]
[[Category: He HT-F]]
[[Category: Isaza, C E]]
[[Category: Isaza CE]]
[[Category: Lee, M M]]
[[Category: Lee MM]]
[[Category: Liang, G F.C]]
[[Category: Liang GF-C]]
[[Category: White, J D]]
[[Category: White JD]]
[[Category: Hydrolase]]
[[Category: Metal-binding]]
[[Category: Metalloprotease]]
[[Category: Protease]]
[[Category: Zinc]]

Latest revision as of 13:01, 21 February 2024

BsuCP Crystal StructureBsuCP Crystal Structure

Structural highlights

3hq2 is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CBP1_BACSU Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues. Has lower activity with substrates ending with His or Trp.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Lee MM, Isaza CE, White JD, Chen RP, Liang GF, He HT, Chan SI, Chan MK. Insight into the substrate length restriction of M32 carboxypeptidases: Characterization of two distinct subfamilies. Proteins. 2009 May 11;77(3):647-657. PMID:19544567 doi:10.1002/prot.22478

3hq2, resolution 2.90Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=3hq2&oldid=4065355"