1nlu

<table><tr><td colspan='2'>[[1nlu]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Achromobacter_georgiopolitanum Achromobacter georgiopolitanum]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1NLU FirstGlance]. <br>

</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></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sedolisin Sedolisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.100 3.4.21.100] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1nlu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nlu OCA], [http://pdbe.org/1nlu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nlu RCSB], [http://www.ebi.ac.uk/pdbsum/1nlu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nlu ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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).

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1nlu" style="background-color:#fffaf0;"></div>

*[[Proteinase|Proteinase]]

== References ==

<references/>

[[Category: Achromobacter georgiopolitanum]]

[[Category: Sedolisin]]

[[Category: Dauter, Z]]

[[Category: Dunn, B M]]

[[Category: Glodfarb, N E]]

[[Category: Gustchina, A]]

[[Category: Li, M]]

[[Category: Oda, K]]

[[Category: Oyama, H]]

[[Category: Uchida, K]]

[[Category: Wlodawer, A]]

[[Category: Pscp]]