3hoa
From Proteopedia
(Difference between revisions)
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<StructureSection load='3hoa' size='340' side='right'caption='[[3hoa]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='3hoa' size='340' side='right'caption='[[3hoa]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3hoa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3hoa]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB27 Thermus thermophilus HB27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HOA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HOA FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=3hoa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hoa OCA], [https://pdbe.org/3hoa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hoa RCSB], [https://www.ebi.ac.uk/pdbsum/3hoa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hoa 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=3hoa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hoa OCA], [https://pdbe.org/3hoa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hoa RCSB], [https://www.ebi.ac.uk/pdbsum/3hoa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hoa ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q72GY3_THET2 Q72GY3_THET2] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=3hoa 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=3hoa 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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 3hoa" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]] | *[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Carboxypeptidase Taq]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Thermus thermophilus HB27]] |
| - | [[Category: Chan | + | [[Category: Chan MK]] |
| - | [[Category: Lee | + | [[Category: Lee MM]] |
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Current revision
Crystal structure of the Thermus thermophilus M32 carboxypeptidase
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