2v3y

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2v3y.png|left|200px]]
+
==HIS361ALA ESCHERICHIA COLI AMINOPEPTIDASE P IN COMPLEX WITH PRODUCT==
 +
<StructureSection load='2v3y' size='340' side='right' caption='[[2v3y]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2v3y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V3Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V3Y FirstGlance]. <br>
 +
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene><br>
 +
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
 +
<tr><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]], [[2v3x|2v3x]], [[2v3z|2v3z]]</td></tr>
 +
<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v3y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v3y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v3y RCSB], [http://www.ebi.ac.uk/pdbsum/2v3y PDBsum]</span></td></tr>
 +
<table>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v3/2v3y_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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/chain_selection.php?pdb_ID=2ata ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== 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.
-
{{STRUCTURE_2v3y| PDB=2v3y | SCENE= }}
+
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<ref>PMID:17983589</ref>
-
===HIS361ALA ESCHERICHIA COLI AMINOPEPTIDASE P IN COMPLEX WITH PRODUCT===
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
 
+
</div>
-
{{ABSTRACT_PUBMED_17983589}}
+
-
 
+
-
==About this Structure==
+
-
[[2v3y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V3Y OCA].
+
==See Also==
==See Also==
*[[Aminopeptidase|Aminopeptidase]]
*[[Aminopeptidase|Aminopeptidase]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:017983589</ref><references group="xtra"/>
+
__TOC__
 +
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Xaa-Pro aminopeptidase]]
[[Category: Xaa-Pro aminopeptidase]]

Revision as of 08:32, 29 September 2014

HIS361ALA ESCHERICHIA COLI AMINOPEPTIDASE P IN COMPLEX WITH PRODUCT

2v3y, resolution 1.60Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2v3y"
Views
Personal tools
Navigation
Toolbox