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1qtr

From Proteopedia

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(New page: 200px<br /><applet load="1qtr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qtr, resolution 2.32&Aring;" /> '''CRYSTAL STRUCTURE AN...)
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[[Image:1qtr.jpg|left|200px]]<br /><applet load="1qtr" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qtr, resolution 2.32&Aring;" />
 
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'''CRYSTAL STRUCTURE ANALYSIS OF THE PROLYL AMINOPEPTIDASE FROM SERRATIA MARCESCENS'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE ANALYSIS OF THE PROLYL AMINOPEPTIDASE FROM SERRATIA MARCESCENS==
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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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<StructureSection load='1qtr' size='340' side='right'caption='[[1qtr]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
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== Structural highlights ==
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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='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'>[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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PIP_SERMA PIP_SERMA] Specifically catalyzes the removal of N-terminal proline residues from peptides.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qt/1qtr_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1QTR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QTR OCA].
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*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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 (Tokyo). 1999 Sep;126(3):559-65. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10467172 10467172]
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[[Category: Large Structures]]
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[[Category: Prolyl aminopeptidase]]
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[[Category: Serratia marcescens]]
[[Category: Serratia marcescens]]
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[[Category: Single protein]]
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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: iminopeptidase]]
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[[Category: proline]]
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[[Category: prolyl aminopeptidase]]
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[[Category: serratia]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:58:41 2007''
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Current revision

CRYSTAL STRUCTURE ANALYSIS OF THE PROLYL AMINOPEPTIDASE FROM SERRATIA MARCESCENS

PDB ID 1qtr

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