4z65: Difference between revisions
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==Carboxypeptidase B with Sulphamoil Arginine== | ==Carboxypeptidase B with Sulphamoil Arginine== | ||
<StructureSection load='4z65' size='340' side='right' caption='[[4z65]], [[Resolution|resolution]] 1.25Å' scene=''> | <StructureSection load='4z65' size='340' side='right'caption='[[4z65]], [[Resolution|resolution]] 1.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4z65]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z65 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z65 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4z65]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z65 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z65 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0X9:N~2~-SULFAMOYL-L-ARGININE'>0X9</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0X9:N~2~-SULFAMOYL-L-ARGININE'>0X9</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CPB1, CPB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxypeptidase_B Carboxypeptidase B], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.2 3.4.17.2] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carboxypeptidase_B Carboxypeptidase B], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.2 3.4.17.2] </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=4z65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z65 OCA], [http://pdbe.org/4z65 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z65 RCSB], [http://www.ebi.ac.uk/pdbsum/4z65 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=4z65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z65 OCA], [http://pdbe.org/4z65 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z65 RCSB], [http://www.ebi.ac.uk/pdbsum/4z65 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4z65 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 4z65" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4z65" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Carboxypeptidase B]] | [[Category: Carboxypeptidase B]] | ||
[[Category: Large Structures]] | |||
[[Category: Pig]] | |||
[[Category: Akparov, V K]] | [[Category: Akparov, V K]] | ||
[[Category: Kuranova, I P]] | [[Category: Kuranova, I P]] | ||
Revision as of 10:15, 19 June 2019
Carboxypeptidase B with Sulphamoil ArginineCarboxypeptidase B with Sulphamoil Arginine
Structural highlights
Publication Abstract from PubMedPorcine pancreatic carboxypeptidase B (EC 3.4.23.6) was complexed with a stable transition-state analogue, N-sulfamoyl-L-arginine, in which an S atom imitates the sp(3)-hybridized carbon in the scissile-bond surrogate. Crystals were grown in a form belonging to the same space group, P41212, as the uncomplexed enzyme. X-ray data were collected to a resolution of 1.25 A. The molecule was refined and the positions of non-H atoms of the inhibitor and water molecules were defined using difference Fourier maps. The enzyme-inhibitor complex and 329 water molecules were further refined to a crystallographic R factor of 0.159. The differences in conformation between the complexed and uncomplexed forms of carboxypeptidase B are shown. The inhibitor is bound in a curved conformation in the active-site cleft, and the sulfamide group is bound to the Zn ion in an asymmetric bidentate fashion. The complex is stabilized by hydrogen bonds between the N1/N2 guanidine group of the inhibitor and the Asp255 carboxyl of the enzyme. The side-chain CH2 groups of the inhibitor are in van der Waals contact with Leu203 and Ile247 in the enzyme. This study provides useful clues concerning how the transition state of arginine may bind to carboxypeptidase B and therefore provides an insight into the structural basis of carboxypeptidase B selectivity, which is useful for the rational design of a carboxypeptidase with improved selectivity for industrial recombinant pro-insulin processing. Structure of the complex of carboxypeptidase B and N-sulfamoyl-L-arginine.,Akparov V, Sokolenko N, Timofeev V, Kuranova I Acta Crystallogr F Struct Biol Commun. 2015 Oct 1;71(Pt 10):1335-40. doi:, 10.1107/S2053230X15016799. Epub 2015 Sep 23. PMID:26457527[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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