1nlu

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{{Seed}}
 
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[[Image:1nlu.png|left|200px]]
 
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==Pseudomonas sedolisin (serine-carboxyl proteinase) complexed with two molecules of pseudo-iodotyrostatin==
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The line below this paragraph, containing "STRUCTURE_1nlu", creates the "Structure Box" on the page.
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<StructureSection load='1nlu' size='340' side='right'caption='[[1nlu]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1nlu]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NLU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NLU FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.3&#8491;</td></tr>
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<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=IVA:ISOVALERIC+ACID'>IVA</scene>, <scene name='pdbligand=PHI:IODO-PHENYLALANINE'>PHI</scene>, <scene name='pdbligand=TYB:TYROSINAL'>TYB</scene></td></tr>
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{{STRUCTURE_1nlu| PDB=1nlu | SCENE= }}
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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=1nlu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nlu OCA], [https://pdbe.org/1nlu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nlu RCSB], [https://www.ebi.ac.uk/pdbsum/1nlu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nlu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PICP_PSESR PICP_PSESR]
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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/nl/1nlu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1nlu ConSurf].
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<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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High-resolution crystallographic analysis of a complex of the serine-carboxyl proteinase sedolisin with pseudo-iodotyrostatin revealed two molecules of this inhibitor bound in the active site of the enzyme, marking subsites from S3 to S3('). The mode of binding represents two products of the proteolytic reaction. Substrate specificity of sedolisin was investigated using peptide libraries and a new peptide substrate for sedolisin, MCA-Lys-Pro-Pro-Leu-Glu#Tyr-Arg-Leu-Gly-Lys(DNP)-Gly, was synthesized based on the results of the enzymatic and crystallographic studies and was shown to be efficiently cleaved by the enzyme. The kinetic parameters for the substrate, measured by the increase in fluorescence upon relief of quenching, were: k(cat)=73+/-5 s(-1), K(m)=0.12+/-0.011 microM, and k(cat)/K(m)=608+/-85 s(-1)microM(-1).
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===Pseudomonas sedolisin (serine-carboxyl proteinase) complexed with two molecules of pseudo-iodotyrostatin===
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Two inhibitor molecules bound in the active site of Pseudomonas sedolisin: a model for the bi-product complex following cleavage of a peptide substrate.,Wlodawer A, Li M, Gustchina A, Oyama H, Oda K, Beyer BB, Clemente J, Dunn BM Biochem Biophys Res Commun. 2004 Feb 6;314(2):638-45. PMID:14733955<ref>PMID:14733955</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 1nlu" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_14733955}}, adds the Publication Abstract to the page
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*[[Pepsin|Pepsin]]
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(as it appears on PubMed at http://www.pubmed.gov), where 14733955 is the PubMed ID number.
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*[[Proteinase 3D structures|Proteinase 3D structures]]
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== References ==
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{{ABSTRACT_PUBMED_14733955}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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1NLU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NLU OCA].
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[[Category: Large Structures]]
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[[Category: Pseudomonas sp]]
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==Reference==
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[[Category: Dauter Z]]
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Two inhibitor molecules bound in the active site of Pseudomonas sedolisin: a model for the bi-product complex following cleavage of a peptide substrate., Wlodawer A, Li M, Gustchina A, Oyama H, Oda K, Beyer BB, Clemente J, Dunn BM, Biochem Biophys Res Commun. 2004 Feb 6;314(2):638-45. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14733955 14733955]
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[[Category: Dunn BM]]
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[[Category: Pseudomonalisin]]
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[[Category: Glodfarb NE]]
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[[Category: Pseudomonas sp.]]
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[[Category: Gustchina A]]
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[[Category: Single protein]]
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[[Category: Li M]]
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[[Category: Dauter, Z.]]
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[[Category: Oda K]]
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[[Category: Dunn, B M.]]
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[[Category: Oyama H]]
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[[Category: Glodfarb, N E.]]
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[[Category: Uchida K]]
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[[Category: Gustchina, A.]]
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[[Category: Wlodawer A]]
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[[Category: Li, M.]]
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[[Category: Oda, K.]]
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[[Category: Oyama, H.]]
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[[Category: Uchida, K.]]
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[[Category: Wlodawer, A.]]
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[[Category: Pscp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:27:30 2008''
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Current revision

Pseudomonas sedolisin (serine-carboxyl proteinase) complexed with two molecules of pseudo-iodotyrostatin

PDB ID 1nlu

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