2pkp

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2pkp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PKP FirstGlance]. <br>
<table><tr><td colspan='2'>[[2pkp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PKP FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aksE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aksE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii])</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methanogen_homoaconitase Methanogen homoaconitase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.114 4.2.1.114] </span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methanogen_homoaconitase Methanogen homoaconitase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.114 4.2.1.114] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pkp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2pkp RCSB], [http://www.ebi.ac.uk/pdbsum/2pkp PDBsum], [http://www.topsan.org/Proteins/RSGI/2pkp TOPSAN]</span></td></tr>
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<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=2pkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pkp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2pkp RCSB], [http://www.ebi.ac.uk/pdbsum/2pkp PDBsum], [http://www.topsan.org/Proteins/RSGI/2pkp TOPSAN]</span></td></tr>
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<table>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/HACB_METJA HACB_METJA]] Hydro-lyase with broad substrate specificity for cis-unsaturated tricarboxylic acids. Catalyzes both the reversible dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4-tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4-tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the analogous longer chain substrates cis-homo(2)-aconitate, cis-homo(3)-aconitate, and even the non-physiological cis-homo(4)-aconitate with similar efficiency. These reactions are part of the biosynthesis pathway of coenzyme B. Can also catalyze the hydration of maleate to (R)-malate, and that of cis-aconitate. Can not catalyze the hydration of citraconate and the dehydration of (S)-homocitrate, citramalate, 2-isopropylmalate, 3-isopropylmalate, citrate or threo-DL-isocitrate.<ref>PMID:17449626</ref> <ref>PMID:18765671</ref> <ref>PMID:20170198</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Methanocaldococcus jannaschii]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Methanogen homoaconitase]]
[[Category: Methanogen homoaconitase]]
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[[Category: Agari, Y.]]
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[[Category: Agari, Y]]
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[[Category: Ebihara, A.]]
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[[Category: Ebihara, A]]
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[[Category: Gayathri, D R.]]
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[[Category: Gayathri, D R]]
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[[Category: Jeyakanthan, J.]]
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[[Category: Jeyakanthan, J]]
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[[Category: Kuramitsu, S.]]
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[[Category: Kuramitsu, S]]
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
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[[Category: Structural genomic]]
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[[Category: Shinkai, A.]]
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[[Category: Shinkai, A]]
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[[Category: Shiro, Y.]]
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[[Category: Shiro, Y]]
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[[Category: Velmurugan, D.]]
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[[Category: Velmurugan, D]]
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[[Category: Yokoyama, S.]]
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[[Category: Yokoyama, S]]
[[Category: Amino-acid biosynthesis]]
[[Category: Amino-acid biosynthesis]]
[[Category: Beta barrel]]
[[Category: Beta barrel]]
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[[Category: National project on protein structural and functional analyse]]
[[Category: National project on protein structural and functional analyse]]
[[Category: Nppsfa]]
[[Category: Nppsfa]]
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[[Category: Riken structural genomics/proteomics initiative]]
 
[[Category: Rsgi]]
[[Category: Rsgi]]
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[[Category: Structural genomic]]
 

Revision as of 22:29, 25 December 2014

Crystal structure of 3-isopropylmalate dehydratase (leuD)from Methhanocaldococcus Jannaschii DSM2661 (MJ1271)

2pkp, resolution 2.10Å

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