1nlu: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older edit
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
 
(11 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1nlu.jpg|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_1nlu", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_1nlu|  PDB=1nlu  |  SCENE=  }}
'''Pseudomonas sedolisin (serine-carboxyl proteinase) complexed with two molecules of pseudo-iodotyrostatin'''


==Pseudomonas sedolisin (serine-carboxyl proteinase) complexed with two molecules of pseudo-iodotyrostatin==
<StructureSection load='1nlu' size='340' side='right'caption='[[1nlu]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PICP_PSESR PICP_PSESR]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nl/1nlu_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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).


==Overview==
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>
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).


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 1nlu" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Pepsin|Pepsin]]
[[Category: Pseudomonalisin]]
*[[Proteinase 3D structures|Proteinase 3D structures]]
[[Category: Pseudomonas sp.]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Dauter, Z.]]
__TOC__
[[Category: Dunn, B M.]]
</StructureSection>
[[Category: Glodfarb, N E.]]
[[Category: Large Structures]]
[[Category: Gustchina, A.]]
[[Category: Pseudomonas sp]]
[[Category: Li, M.]]
[[Category: Dauter Z]]
[[Category: Oda, K.]]
[[Category: Dunn BM]]
[[Category: Oyama, H.]]
[[Category: Glodfarb NE]]
[[Category: Uchida, K.]]
[[Category: Gustchina A]]
[[Category: Wlodawer, A.]]
[[Category: Li M]]
[[Category: Pscp]]
[[Category: Oda K]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:41:03 2008''
[[Category: Oyama H]]
[[Category: Uchida K]]
[[Category: Wlodawer A]]
Retrieved from "https://proteopedia.org/1nlu"