1qtr

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<StructureSection load='1qtr' size='340' side='right'caption='[[1qtr]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
<StructureSection load='1qtr' size='340' side='right'caption='[[1qtr]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1qtr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_marcescens"_(bizio_1823)_trevisan_in_de_toni_and_trevisan_1889 "bacillus marcescens" (bizio 1823) trevisan in de toni and trevisan 1889]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QTR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QTR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1qtr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QTR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QTR FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] </span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.32&#8491;</td></tr>
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<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=1qtr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qtr OCA], [http://pdbe.org/1qtr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qtr RCSB], [http://www.ebi.ac.uk/pdbsum/1qtr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qtr ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qtr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qtr OCA], [https://pdbe.org/1qtr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qtr RCSB], [https://www.ebi.ac.uk/pdbsum/1qtr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qtr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PIP_SERMA PIP_SERMA]] Specifically catalyzes the removal of N-terminal proline residues from peptides.
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[https://www.uniprot.org/uniprot/PIP_SERMA PIP_SERMA] Specifically catalyzes the removal of N-terminal proline residues from peptides.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1qtr 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=1qtr ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Prolyl aminopeptidase from Serratia marcescens specifically catalyzes the removal of N-terminal proline residues from peptides. We have solved its three-dimensional structure at 2.3 A resolution by the multiple isomorphous replacement method. The enzyme consists of two contiguous domains. The larger domain shows the general topology of the alpha/beta hydrolase fold, with a central eight-stranded beta-sheet and six helices. The smaller domain consists of six helices. The catalytic triad (Ser113, His296, and Asp268) is located near the large cavity at the interface between the two domains. Cys271, which is sensitive to SH reagents, is located near the catalytic residues, in spite of the fact that the enzyme is a serine peptidase. The specific residues which make up the hydrophobic pocket line the smaller domain, and the specificity of the exo-type enzyme originates from this smaller domain, which blocks the N-terminal of P1 proline.
 
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Crystal structure of prolyl aminopeptidase from Serratia marcescens.,Yoshimoto T, Kabashima T, Uchikawa K, Inoue T, Tanaka N, Nakamura KT, Tsuru M, Ito K J Biochem. 1999 Sep;126(3):559-65. PMID:10467172<ref>PMID:10467172</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1qtr" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Prolyl aminopeptidase]]
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[[Category: Serratia marcescens]]
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[[Category: Inoue, T]]
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[[Category: Inoue T]]
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[[Category: Kabashima, T]]
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[[Category: Kabashima T]]
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[[Category: Tanaka, N]]
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[[Category: Tanaka N]]
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[[Category: Uchikawa, K]]
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[[Category: Uchikawa K]]
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[[Category: Yoshimoto, T]]
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[[Category: Yoshimoto T]]
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[[Category: Alpha beta hydrolase fold]]
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[[Category: Hydrolase]]
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[[Category: Iminopeptidase]]
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[[Category: Proline]]
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[[Category: Serratia]]
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Current revision

CRYSTAL STRUCTURE ANALYSIS OF THE PROLYL AMINOPEPTIDASE FROM SERRATIA MARCESCENS

PDB ID 1qtr

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