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3kxp
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3kxp is ON HOLD Authors: McCulloch, K.M., Mukherjee, T., Begley, T.P., Ealick, S.E. Description: Crystal Structure of E-2-(Acetamidomethylene)succi...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of E-2-(Acetamidomethylene)succinate Hydrolase== | |
| + | <StructureSection load='3kxp' size='340' side='right' caption='[[3kxp]], [[Resolution|resolution]] 2.26Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3kxp]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_700743 Atcc 700743]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KXP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3KXP FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">5331 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=381 ATCC 700743])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3kxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kxp OCA], [http://pdbe.org/3kxp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3kxp RCSB], [http://www.ebi.ac.uk/pdbsum/3kxp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3kxp ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/kx/3kxp_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=3kxp ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The gene identification and kinetic characterization of (E)-2-(acetamidomethylene)succinate (E-2AMS) hydrolase has recently been described. This enzyme catalyzes the final reaction in the degradation of vitamin B(6) and produces succinic semialdehyde, acetate, ammonia, and carbon dioxide from E-2AMS. The structure of E-2AMS hydrolase was determined to 2.3 A using SAD phasing. E-2AMS hydrolase is a member of the alpha/beta hydrolase superfamily and utilizes a serine/histidine/aspartic acid catalytic triad. Mutation of either the nucleophilic serine or the aspartate resulted in inactive enzyme. Mutation of an additional serine residue in the active site causes the enzyme to be unstable and is likely structurally important. The structure also provides insight into the mechanism of hydrolysis of E-2AMS and identifies several potential catalytically important residues. | ||
| - | + | Structure Determination and Characterization of the Vitamin B(6) Degradative Enzyme (E)-2-(Acetamidomethylene)succinate Hydrolase (,).,McCulloch KM, Mukherjee T, Begley TP, Ealick SE Biochemistry. 2010 Feb 16;49(6):1226-35. PMID:20099871<ref>PMID:20099871</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3kxp" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Atcc 700743]] | ||
| + | [[Category: Begley, T P]] | ||
| + | [[Category: Ealick, S E]] | ||
| + | [[Category: McCulloch, K M]] | ||
| + | [[Category: Mukherjee, T]] | ||
| + | [[Category: Alpha/beta hydrolase]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Plp degradation]] | ||
Current revision
Crystal Structure of E-2-(Acetamidomethylene)succinate Hydrolase
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