3b7r: Difference between revisions

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-{{Seed}}
-[[Image:3b7r.jpg|left|200px]]
-<!--
+==Leukotriene A4 Hydrolase Complexed with Inhibitor RB3040==
-The line below this paragraph, containing "STRUCTURE_3b7r", creates the "Structure Box" on the page.
+<StructureSection load='3b7r' size='340' side='right'caption='[[3b7r]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3b7r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B7R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B7R FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.811&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BIR:N-[3-[(1-AMINOETHYL)(HYDROXY)PHOSPHORYL]-2-(1,1-BIPHENYL-4-YLMETHYL)PROPANOYL]ALANINE'>BIR</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=YB:YTTERBIUM+(III)+ION'>YB</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-{{STRUCTURE_3b7r|  PDB=3b7r  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3b7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b7r OCA], [https://pdbe.org/3b7r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b7r RCSB], [https://www.ebi.ac.uk/pdbsum/3b7r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b7r ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/LKHA4_HUMAN LKHA4_HUMAN] Epoxide hydrolase that catalyzes the final step in the biosynthesis of the proinflammatory mediator leukotriene B4. Has also aminopeptidase activity.<ref>PMID:1897988</ref> <ref>PMID:1975494</ref> <ref>PMID:2244921</ref> <ref>PMID:12207002</ref> <ref>PMID:11917124</ref> <ref>PMID:15078870</ref> <ref>PMID:18804029</ref>
+== 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/b7/3b7r_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3b7r ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+M1 aminopeptidases comprise a large family of biologically important zinc enzymes. We show that peptide turnover by the M1 prototype, leukotriene A4 hydrolase/aminopeptidase, involves a shift in substrate position associated with exchange of zinc coordinating groups, while maintaining the overall coordination geometry. The transition state is stabilized by residues conserved among M1 members and in the final reaction step, Glu-296 of the canonical zinc binding HEXXH motif shuffles a proton from the hydrolytic water to the leaving group. Tripeptide substrates bind along the conserved GXMEN motif, precisely occupying the distance between Glu-271 and Arg-563, whereas the Arg specificity is governed by a narrow S1 pocket capped with Asp-375. Our data provide detailed insights to the active site chemistry of M1 aminopeptidases and will aid in the development of novel enzyme inhibitors.
-===Leukotriene A4 Hydrolase Complexed with Inhibitor RB3040===
+Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: implications for M1 aminopeptidases and inhibitor design.,Tholander F, Muroya A, Roques BP, Fournie-Zaluski MC, Thunnissen MM, Haeggstrom JZ Chem Biol. 2008 Sep 22;15(9):920-9. PMID:18804029<ref>PMID:18804029</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3b7r" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_17357161}}, adds the Publication Abstract to the page
+*[[Leukotriene A4 Hydrolase|Leukotriene A4 Hydrolase]]
-(as it appears on PubMed at http://www.pubmed.gov), where 17357161 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_17357161}}
+__TOC__
+</StructureSection>
-==About this Structure==
-B7R is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B7R OCA].
-==Reference==
-Assay for rapid analysis of the tri-peptidase activity of LTA4 hydrolase., Tholander F, Haeggstrom JZ, Proteins. 2007 Jun 1;67(4):1113-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17357161 17357161]
-Leukotriene A4 hydrolase: identification of a common carboxylate recognition site for the epoxide hydrolase and aminopeptidase substrates., Rudberg PC, Tholander F, Andberg M, Thunnissen MM, Haeggstrom JZ, J Biol Chem. 2004 Jun 25;279(26):27376-82. Epub 2004 Apr 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15078870 15078870]
-Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms., Rudberg PC, Tholander F, Thunnissen MM, Haeggstrom JZ, J Biol Chem. 2002 Jan 11;277(2):1398-404. Epub 2001 Oct 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11675384 11675384]
-Leukotriene A4 hydrolase: selective abrogation of leukotriene B4 formation by mutation of aspartic acid 375., Rudberg PC, Tholander F, Thunnissen MM, Samuelsson B, Haeggstrom JZ, Proc Natl Acad Sci U S A. 2002 Apr 2;99(7):4215-20. Epub 2002 Mar 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11917124 11917124]
-Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation., Thunnissen MM, Nordlund P, Haeggstrom JZ, Nat Struct Biol. 2001 Feb;8(2):131-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11175901 11175901]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Fournie-Zaluski, M C.]]
+[[Category: Fournie-Zaluski M-C]]
-[[Category: Haeggstrom, J.]]
+[[Category: Haeggstrom J]]
-[[Category: Muroya, A.]]
+[[Category: Muroya A]]
-[[Category: Roques, B P.]]
+[[Category: Roques B-P]]
-[[Category: Tholander, F.]]
+[[Category: Tholander F]]
-[[Category: Thunnissen, M.]]
+[[Category: Thunnissen M]]
-[[Category: Alternative splicing]]
-[[Category: Analogue peptide]]
-[[Category: Cytoplasm]]
-[[Category: Hydrolase]]
-[[Category: Hydrolysis]]
-[[Category: Leukotriene biosynthesis]]
-[[Category: Metal-binding]]
-[[Category: Metalloprotease]]
-[[Category: Multifunctional enzyme]]
-[[Category: Protease]]
-[[Category: Transition state]]
-[[Category: Zinc]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 17 14:22:45 2008''