3b7w: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3b7w]] is a 1 chain structure with 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=3B7W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3B7W FirstGlance]. <br> | <table><tr><td colspan='2'>[[3b7w]] is a 1 chain structure with 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=3B7W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3B7W FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACSM2A, ACSM2, MACS2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACSM2A, ACSM2, MACS2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Butyrate--CoA_ligase Butyrate--CoA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.2 6.2.1.2] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Butyrate--CoA_ligase Butyrate--CoA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.2 6.2.1.2] </span></td></tr> | ||
<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=3b7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b7w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3b7w RCSB], [http://www.ebi.ac.uk/pdbsum/3b7w PDBsum]</span></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=3b7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b7w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3b7w RCSB], [http://www.ebi.ac.uk/pdbsum/3b7w PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/ACS2A_HUMAN ACS2A_HUMAN]] Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4-unsaturated acids (in vitro) (By similarity). | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Butyrate--CoA ligase]] | [[Category: Butyrate--CoA ligase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Arrowsmith, C H | [[Category: Arrowsmith, C H]] | ||
[[Category: Delft, F Von | [[Category: Delft, F Von]] | ||
[[Category: Edwards, A M | [[Category: Edwards, A M]] | ||
[[Category: Kochan, G T | [[Category: Kochan, G T]] | ||
[[Category: Oppermann, U | [[Category: Oppermann, U]] | ||
[[Category: Pike, A C.W | [[Category: Pike, A C.W]] | ||
[[Category: Pilka, E S | [[Category: Pilka, E S]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Weigelt, J | [[Category: Weigelt, J]] | ||
[[Category: Atp-binding]] | [[Category: Atp-binding]] | ||
[[Category: Fatty acid metabolism]] | [[Category: Fatty acid metabolism]] | ||
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[[Category: Nucleotide-binding]] | [[Category: Nucleotide-binding]] | ||
[[Category: Sgc]] | [[Category: Sgc]] | ||
[[Category: Transit peptide]] | [[Category: Transit peptide]] | ||
[[Category: Xenobiotic/medium-chain fatty acid-coa ligase]] | [[Category: Xenobiotic/medium-chain fatty acid-coa ligase]] | ||
Revision as of 07:49, 25 December 2014
Crystal structure of human acyl-CoA synthetase medium-chain family member 2A, with L64P mutationCrystal structure of human acyl-CoA synthetase medium-chain family member 2A, with L64P mutation
Structural highlights
Function[ACS2A_HUMAN] Has medium-chain fatty acid:CoA ligase activity with broad substrate specificity (in vitro). Acts on acids from C(4) to C(11) and on the corresponding 3-hydroxy- and 2,3- or 3,4-unsaturated acids (in vitro) (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAcyl-CoA synthetases belong to the superfamily of adenylate-forming enzymes, and catalyze the two-step activation of fatty acids or carboxylate-containing xenobiotics. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Here, we report the first crystal structure of a medium-chain acyl-CoA synthetase ACSM2A, in a series of substrate/product/cofactor complexes central to the catalytic mechanism. We observed a substantial rearrangement between the N- and C-terminal domains, driven purely by the identity of the bound ligand in the active site. Our structures allowed us to identify the presence or absence of the ATP pyrophosphates as the conformational switch, and elucidated new mechanistic details, including the role of invariant Lys557 and a divalent magnesium ion in coordinating the ATP pyrophosphates, as well as the involvement of a Gly-rich P-loop and the conserved Arg472-Glu365 salt bridge in the domain rearrangement. Structural snapshots for the conformation-dependent catalysis by human medium-chain acyl-coenzyme A synthetase ACSM2A.,Kochan G, Pilka ES, von Delft F, Oppermann U, Yue WW J Mol Biol. 2009 May 22;388(5):997-1008. Epub 2009 Apr 1. PMID:19345228[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Butyrate--CoA ligase
- Homo sapiens
- Arrowsmith, C H
- Delft, F Von
- Edwards, A M
- Kochan, G T
- Oppermann, U
- Pike, A C.W
- Pilka, E S
- Structural genomic
- Weigelt, J
- Atp-binding
- Fatty acid metabolism
- Ligase
- Lipid metabolism
- Magnesium
- Metal-binding
- Middle-chain acyl-coa synthetase
- Mitochondrion
- Nucleotide-binding
- Sgc
- Transit peptide
- Xenobiotic/medium-chain fatty acid-coa ligase