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[[Image:2v3x.jpg|left|200px]]


{{Structure
==His243Ala Escherichia coli aminopeptidase P in complex with substrate==
|PDB= 2v3x |SIZE=350|CAPTION= <scene name='initialview01'>2v3x</scene>, resolution 1.70&Aring;
<StructureSection load='2v3x' size='340' side='right'caption='[[2v3x]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
|SITE= <scene name='pdbsite=AC1:Mn+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Mn+Binding+Site+For+Chain+A'>AC2</scene> and <scene name='pdbsite=AC3:Cl+Binding+Site+For+Chain+A'>AC3</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>
<table><tr><td colspan='2'>[[2v3x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V3X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V3X FirstGlance]. <br>
|ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
|GENE=
<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=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v3x OCA], [https://pdbe.org/2v3x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v3x RCSB], [https://www.ebi.ac.uk/pdbsum/2v3x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v3x ProSAT]</span></td></tr>
|RELATEDENTRY=[[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]]
</table>
|RESOURCES=<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://www.ebi.ac.uk/pdbsum/2v3x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2v3x RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/AMPP_ECOLI AMPP_ECOLI]
== 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/v3/2v3x_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/main_output.php?pdb_ID=2v3x 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.


'''HIS243ALA ESCHERICHIA COLI AMINOPEPTIDASE P IN COMPLEX WITH SUBSTRATE'''
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>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2v3x" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
 
== References ==
==About this Structure==
<references/>
2V3X is a [[Protein complex]] structure of sequences 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=2V3X OCA].
__TOC__
 
</StructureSection>
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/17983589 17983589]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Xaa-Pro aminopeptidase]]
[[Category: Graham SC]]
[[Category: Graham, S C.]]
[[Category: Guss JM]]
[[Category: Guss, J M.]]
[[Category: pita-bread enzyme]]
[[Category: aminopeptidase]]
[[Category: aminopeptidase p]]
[[Category: hydrolase]]
[[Category: manganese]]
[[Category: manganese enzyme]]
[[Category: metal-binding]]
[[Category: metalloenzyme]]
[[Category: metalloprotease]]
[[Category: proline- specific enzyme]]
[[Category: protease]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:08:14 2008''

Latest revision as of 08:31, 17 October 2024

His243Ala Escherichia coli aminopeptidase P in complex with substrateHis243Ala Escherichia coli aminopeptidase P in complex with substrate

Structural highlights

2v3x is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AMPP_ECOLI

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.

See Also

References

  1. ↑ 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

2v3x, resolution 1.70Å

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