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2v3x

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Revision as of 08:12, 12 September 2018

His243Ala Escherichia coli aminopeptidase P in complex with substrate

Structural highlights

2v3x is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Related:	1a16, 1jaw, 1m35, 1n51, 1w2m, 1w7v, 1wbq, 1wl6, 1wl9, 1wlr, 2bh3, 2bha, 2bhb, 2bhc, 2bhd, 2bn7, 2bws, 2bwt, 2bwu, 2bwv, 2bww, 2bwx, 2bwy, 2v3y, 2v3z
Activity:	Xaa-Pro aminopeptidase, with EC number 3.4.11.9
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

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

Publication Abstract from PubMed

Aminopeptidase P (APPro) is a manganese-containing enzyme that catalyses the hydrolysis of the N-terminal residue of a polypeptide if the second residue is proline. Structures of APPro mutants with reduced or negligible activity have been determined in complex with the tripeptide substrate ValProLeu. In the complex of Glu383Ala APPro with ValProLeu one of the two metal sites is only partly occupied, indicating an essential role for Glu383 in metal binding in the presence of substrate. His361Ala APPro clearly possesses residual activity as the ValProLeu substrate has been cleaved in the crystals; difference electron density consistent with bound ProLeu dipeptide and a disordered Val amino acid is present at the active site. Contrary to previous suggestions, the His243Ala mutant is capable of binding substrate. The structure of the His243Ala APPro complex with ValProLeu shows that the peptide interacts with one of the active-site metal atoms via its terminal amino group. The implications of these complexes for the roles of the respective residues in APPro catalysis are discussed.

Complexes of mutants of Escherichia coli aminopeptidase P and the tripeptide substrate ValProLeu.,Graham SC, Guss JM Arch Biochem Biophys. 2008 Jan 15;469(2):200-8. Epub 2007 Oct 24. PMID:17983589^[1]

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

References

↑ Graham SC, Guss JM. Complexes of mutants of Escherichia coli aminopeptidase P and the tripeptide substrate ValProLeu. Arch Biochem Biophys. 2008 Jan 15;469(2):200-8. Epub 2007 Oct 24. PMID:17983589 doi:http://dx.doi.org/10.1016/j.abb.2007.10.009

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2v3x"

@@ Line 1: / Line 1: @@
-==HIS243ALA ESCHERICHIA COLI AMINOPEPTIDASE P IN COMPLEX WITH SUBSTRATE==
+==His243Ala Escherichia coli aminopeptidase P in complex with substrate==
 <StructureSection load='2v3x' size='340' side='right' caption='[[2v3x]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
@@ Line 7: / Line 8: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a16|1a16]], [[1jaw|1jaw]], [[1m35|1m35]], [[1n51|1n51]], [[1w2m|1w2m]], [[1w7v|1w7v]], [[1wbq|1wbq]], [[1wl6|1wl6]], [[1wl9|1wl9]], [[1wlr|1wlr]], [[2bh3|2bh3]], [[2bha|2bha]], [[2bhb|2bhb]], [[2bhc|2bhc]], [[2bhd|2bhd]], [[2bn7|2bn7]], [[2bws|2bws]], [[2bwt|2bwt]], [[2bwu|2bwu]], [[2bwv|2bwv]], [[2bww|2bww]], [[2bwx|2bwx]], [[2bwy|2bwy]], [[2v3y|2v3y]], [[2v3z|2v3z]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xaa-Pro_aminopeptidase Xaa-Pro aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.9 3.4.11.9] </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=2v3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v3x OCA], [http://pdbe.org/2v3x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v3x RCSB], [http://www.ebi.ac.uk/pdbsum/2v3x 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=2v3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v3x OCA], [http://pdbe.org/2v3x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2v3x RCSB], [http://www.ebi.ac.uk/pdbsum/2v3x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2v3x ProSAT]</span></td></tr>
 </table>
 == Evolutionary Conservation ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v3/2v3x_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v3/2v3x_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2v3x

From Proteopedia

Revision as of 08:12, 12 September 2018

His243Ala Escherichia coli aminopeptidase P in complex with substrate

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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