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1s2b

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[[Image:1s2b.jpg|left|200px]]
 
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{{Structure
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==Structure of SCP-B the first member of the Eqolisin family of Peptidases to have its structure determined==
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|PDB= 1s2b |SIZE=350|CAPTION= <scene name='initialview01'>1s2b</scene>, resolution 2.1&Aring;
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<StructureSection load='1s2b' size='340' side='right'caption='[[1s2b]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1s2b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Scytalidium_lignicola Scytalidium lignicola]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S2B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S2B FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Scytalidopepsin_B Scytalidopepsin B], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.32 3.4.23.32] </span>
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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]] 2.1&#8491;</td></tr>
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|GENE=
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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=1s2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s2b OCA], [https://pdbe.org/1s2b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s2b RCSB], [https://www.ebi.ac.uk/pdbsum/1s2b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s2b ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1s2k|1s2k]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s2b OCA], [http://www.ebi.ac.uk/pdbsum/1s2b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1s2b RCSB]</span>
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[https://www.uniprot.org/uniprot/PRTB_SCYLI PRTB_SCYLI]
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}}
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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/s2/1s2b_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=1s2b ConSurf].
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<div style="clear:both"></div>
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'''Structure of SCP-B the first member of the Eqolisin family of Peptidases to have its structure determined'''
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==See Also==
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*[[Pepsin|Pepsin]]
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__TOC__
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==Overview==
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</StructureSection>
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The molecular structure of the pepstatin-insensitive carboxyl peptidase from Scytalidium lignicolum, formerly known as scytalidopepsin B, was solved by multiple isomorphous replacement phasing methods and refined to an R factor of 0.230 (R(free) = 0.246) at 2.1-A resolution. In addition to the structure of the unbound peptidase, the structure of a product complex of cleaved angiotensin II bound in the active site of the enzyme was also determined. We propose the name scytalidocarboxyl peptidase B (SCP-B) for this enzyme. On the basis of conserved, catalytic residues identified at the active site, we suggest the name Eqolisin for the enzyme family. The previously uninvestigated SCP-B fold is that of a beta-sandwich; each sheet has seven antiparallel strands. A tripeptide product, Ala-Ile-His, bound in the active site of SCP-B has allowed for identification of the catalytic residues and the residues in subsites S1, S2, and S3, which are important for substrate binding. The most likely hydrolytic mechanism involves nucleophilic attack of a general base (Glu-136)-activated water (OH(-)) on the si-face of the scissile peptide carbonylcarbon atom to form a tetrahedral intermediate. Electrophilic assistance and oxyanion stabilization is provided by the side-chain amide of Gln-53. Protonation of the leaving-group nitrogen is accomplished by the general acid function of the protonated carboxyl group of Glu-136.
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[[Category: Large Structures]]
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==About this Structure==
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1S2B is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Scytalidium_lignicola Scytalidium lignicola]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S2B OCA].
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==Reference==
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The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum., Fujinaga M, Cherney MM, Oyama H, Oda K, James MN, Proc Natl Acad Sci U S A. 2004 Mar 9;101(10):3364-9. Epub 2004 Mar 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14993599 14993599]
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[[Category: Scytalidium lignicola]]
[[Category: Scytalidium lignicola]]
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[[Category: Scytalidopepsin B]]
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[[Category: Cherney MM]]
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[[Category: Single protein]]
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[[Category: Fujinaga M]]
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[[Category: Cherney, M M.]]
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[[Category: James MN]]
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[[Category: Fujinaga, M.]]
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[[Category: Oda K]]
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[[Category: James, M N.]]
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[[Category: Oyama H]]
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[[Category: Oda, K.]]
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[[Category: Oyama, H.]]
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[[Category: beta sandwich]]
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[[Category: carboxyl peptidase]]
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[[Category: eqolisin family]]
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[[Category: protease]]
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[[Category: proteinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:36:22 2008''
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Current revision

Structure of SCP-B the first member of the Eqolisin family of Peptidases to have its structure determined

PDB ID 1s2b

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