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1xjo

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STRUCTURE OF AMINOPEPTIDASE

Structural highlights

1xjo is a 1 chain structure with sequence from Streptomyces griseus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.75Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

APX_STRGG An exopeptidase specific for larger hydrophobic amino acids (especially leucine), no cleavage occurs if the next residue is proline (PubMed:8444149).^[1] ^[2] ^[3]

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

The X-ray crystal structure of the enzyme Streptomyces griseus aminopeptidase (SGAP) has been determined in its double zinc form to 1.75 A resolution, in its apo-enzyme from (zinc removed) to 2.1 A resolution, and as a mercury replaced derivative to 2.1 A resolution. The structure solution was achieved by single isomorphous replacement with phasing from anomalous scattering (SIRAS), followed by density modification with histogram matching. The protein consists of a central beta-sheet made up of eight parallel and antiparallel strands, surrounded by helices on either side. The active site is located at the carbonyl ends of two middle strands of the beta-sheet region. Two sections of the chain that could not be traced were Glu196 to Arg202, which borders the active site, and the final seven C-terminal residues starting with Gly278. The active site contains two zinc cations, each with similar ligands, at a distance of 3.6 A from each other. An unknown molecule appears to be bound to both zinc ions in the active site at partial occupancy and has been modelled as a phosphate ion. A calcium binding site has also been identified, consistent with the observations that calcium modulates the activity of the enzyme, and increases its heat stability. The mechanism by which the calcium cation modulates enzyme activity is not apparent, since the location of the calcium binding site is approximately 25 A distant from the active site zinc ions. Comparison of the structure of SGAP to other known aminopeptidases shows that the enzyme is most similar to Aeromonas proteolytica aminopeptidase (AAP). Both enzymes share a similar topology, although the overall sequence identity is very low (24% in aligned regions). The coordination of the two active site zinc cations in SGAP resembles that of AAP. These two microbial enzymes differ from bovine lens leucine aminopeptidase (LAP) in both overall structure and in coordination of the two zinc ions.

Streptomyces griseus aminopeptidase: X-ray crystallographic structure at 1.75 A resolution.,Greenblatt HM, Almog O, Maras B, Spungin-Bialik A, Barra D, Blumberg S, Shoham G J Mol Biol. 1997 Feb 7;265(5):620-36. PMID:9048953^[4]

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

References

↑ Spungin A, Blumberg S. Streptomyces griseus aminopeptidase is a calcium-activated zinc metalloprotein. Purification and properties of the enzyme. Eur J Biochem. 1989 Aug 1;183(2):471-7. PMID:2503378 doi:10.1111/j.1432-1033.1989.tb14952.x
↑ Ben-Meir D, Spungin A, Ashkenazi R, Blumberg S. Specificity of Streptomyces griseus aminopeptidase and modulation of activity by divalent metal ion binding and substitution. Eur J Biochem. 1993 Feb 15;212(1):107-12. PMID:8444149 doi:10.1111/j.1432-1033.1993.tb17639.x
↑ Maras B, Greenblatt HM, Shoham G, Spungin-Bialik A, Blumberg S, Barra D. Aminopeptidase from Streptomyces griseus: primary structure and comparison with other zinc-containing aminopeptidases. Eur J Biochem. 1996 Mar 15;236(3):843-6. PMID:8665903 doi:10.1111/j.1432-1033.1996.00843.x
↑ Greenblatt HM, Almog O, Maras B, Spungin-Bialik A, Barra D, Blumberg S, Shoham G. Streptomyces griseus aminopeptidase: X-ray crystallographic structure at 1.75 A resolution. J Mol Biol. 1997 Feb 7;265(5):620-36. PMID:9048953 doi:S0022-2836(96)90729-9

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1xjo"

@@ Line 1: / Line 1: @@
 ==STRUCTURE OF AMINOPEPTIDASE==
-<StructureSection load='1xjo' size='340' side='right' caption='[[1xjo]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+<StructureSection load='1xjo' size='340' side='right'caption='[[1xjo]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1xjo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_griseus"_krainsky_1914 "actinomyces griseus" krainsky 1914]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XJO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XJO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1xjo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_griseus Streptomyces griseus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XJO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XJO FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MHO:S-OXYMETHIONINE'>MHO</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MHO:S-OXYMETHIONINE'>MHO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1xjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xjo OCA], [http://pdbe.org/1xjo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xjo RCSB], [http://www.ebi.ac.uk/pdbsum/1xjo PDBsum]</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=1xjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xjo OCA], [https://pdbe.org/1xjo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xjo RCSB], [https://www.ebi.ac.uk/pdbsum/1xjo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xjo ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/APX_STRGR APX_STRGR]] Specific for larger hydrophobic acids, especially leucine. No cleavage occurs if the next residue is proline.
+[https://www.uniprot.org/uniprot/APX_STRGG APX_STRGG] An exopeptidase specific for larger hydrophobic amino acids (especially leucine), no cleavage occurs if the next residue is proline (PubMed:8444149).<ref>PMID:2503378</ref> <ref>PMID:8444149</ref> <ref>PMID:8665903</ref>
 == 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/xj/1xjo_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xj/1xjo_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].
+</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=1xjo ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 30: / Line 31: @@
 ==See Also==
-*[[Aminopeptidase|Aminopeptidase]]
+*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
 *[[Streptomyces griseus Aminopeptidase (SGAP)|Streptomyces griseus Aminopeptidase (SGAP)]]
 == References ==
@@ Line 36: / Line 37: @@
 __TOC__
 </StructureSection>
-[[Category: Actinomyces griseus krainsky 1914]]
+[[Category: Large Structures]]
-[[Category: Barra, D]]
+[[Category: Streptomyces griseus]]
-[[Category: Blumberg, S]]
+[[Category: Barra D]]
-[[Category: Greenblatt, H M]]
+[[Category: Blumberg S]]
-[[Category: Shoham, G]]
+[[Category: Greenblatt HM]]
-[[Category: Aminopeptidase]]
+[[Category: Shoham G]]
-[[Category: Hydrolase]]
-[[Category: Zymogen]]

1xjo

From Proteopedia

Current revision

STRUCTURE OF AMINOPEPTIDASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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