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==Crystal structure of homoaconitase large subunit from methanococcus jannaschii (MJ1003)==
==Crystal structure of homoaconitase large subunit from methanococcus jannaschii (MJ1003)==
<StructureSection load='4kp2' size='340' side='right' caption='[[4kp2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='4kp2' size='340' side='right'caption='[[4kp2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4kp2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Metja Metja]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KP2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KP2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4kp2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii_DSM_2661 Methanocaldococcus jannaschii DSM 2661]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KP2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KP2 FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hacA, MJ1003 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243232 METJA])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.504&#8491;</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=4kp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kp2 OCA], [http://pdbe.org/4kp2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4kp2 RCSB], [http://www.ebi.ac.uk/pdbsum/4kp2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4kp2 ProSAT]</span></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=4kp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kp2 OCA], [https://pdbe.org/4kp2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kp2 RCSB], [https://www.ebi.ac.uk/pdbsum/4kp2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kp2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/HACA_METJA HACA_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>
[https://www.uniprot.org/uniprot/HACA_METJA HACA_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>  
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Metja]]
[[Category: Large Structures]]
[[Category: Hwang, K Y]]
[[Category: Methanocaldococcus jannaschii DSM 2661]]
[[Category: Lee, E H]]
[[Category: Hwang KY]]
[[Category: Aconitase family]]
[[Category: Lee EH]]
[[Category: Alpha-beta-alpha 3-layer sandwich]]
[[Category: Iron-sulfur cluster binding]]
[[Category: Isomerase]]
[[Category: Lyase]]
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