2vjo: Difference between revisions
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[[Image:2vjo.jpg|left|200px]] | [[Image:2vjo.jpg|left|200px]] | ||
'''FORMYL-COA TRANSFERASE MUTANT VARIANT Q17A WITH ASPARTYL-COA THIOESTER INTERMEDIATES AND OXALATE''' | {{Structure | ||
|PDB= 2vjo |SIZE=350|CAPTION= <scene name='initialview01'>2vjo</scene>, resolution 2.20Å | |||
|SITE= <scene name='pdbsite=AC1:Coa+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Cl+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Coa+Binding+Site+For+Chain+B'>AC3</scene>, <scene name='pdbsite=AC4:Cl+Binding+Site+For+Chain+B'>AC4</scene>, <scene name='pdbsite=AC5:Oxl+Binding+Site+For+Chain+A'>AC5</scene> and <scene name='pdbsite=AC6:Epe+Binding+Site+For+Chain+A'>AC6</scene> | |||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=OXL:OXALATE+ION'>OXL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene> and <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID'>EPE</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Formyl-CoA_transferase Formyl-CoA transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.3.16 2.8.3.16] | |||
|GENE= | |||
}} | |||
'''FORMYL-COA TRANSFERASE MUTANT VARIANT Q17A WITH ASPARTYL-COA THIOESTER INTERMEDIATES AND OXALATE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2VJO is a [ | 2VJO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Oxalobacter_formigenes Oxalobacter formigenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VJO OCA]. | ||
==Reference== | ==Reference== | ||
Reinvestigation of the Catalytic Mechanism of Formyl-CoA Transferase, a Class III CoA-transferase., Berthold CL, Toyota CG, Richards NG, Lindqvist Y, J Biol Chem. 2008 Mar 7;283(10):6519-29. Epub 2007 Dec 27. PMID:[http:// | Reinvestigation of the Catalytic Mechanism of Formyl-CoA Transferase, a Class III CoA-transferase., Berthold CL, Toyota CG, Richards NG, Lindqvist Y, J Biol Chem. 2008 Mar 7;283(10):6519-29. Epub 2007 Dec 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18162462 18162462] | ||
[[Category: Formyl-CoA transferase]] | [[Category: Formyl-CoA transferase]] | ||
[[Category: Oxalobacter formigenes]] | [[Category: Oxalobacter formigenes]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:47:20 2008'' | ||
Revision as of 19:47, 20 March 2008
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , and | ||||||
| Ligands: | , , and | ||||||
| Activity: | Formyl-CoA transferase, with EC number 2.8.3.16 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
FORMYL-COA TRANSFERASE MUTANT VARIANT Q17A WITH ASPARTYL-COA THIOESTER INTERMEDIATES AND OXALATE
OverviewOverview
Formyl-coenzyme A transferase from Oxalobacter formigenes belongs to the Class III coenzyme A transferase family and catalyzes the reversible transfer of a CoA carrier between formyl-CoA and oxalate, forming oxalyl-CoA and formate. Formyl-CoA transferase has a unique three-dimensional fold composed of two interlaced subunits locked together like rings of a chain. We here present an intermediate in the reaction, formyl-CoA transferase containing the covalent beta-aspartyl-CoA thioester, adopting different conformations in the two active sites of the dimer, which was identified through crystallographic freeze-trapping experiments with formyl-CoA and oxalyl-CoA in the absence of acceptor carboxylic acid. The formation of the enzyme-CoA thioester was also confirmed by mass spectrometric data. Further structural data include a trapped aspartyl-formyl anhydride protected by a glycine loop closing down over the active site. In a crystal structure of the beta-aspartyl-CoA thioester of an inactive mutant variant, oxalate was found bound to the open conformation of the glycine loop. Together with hydroxylamine trapping experiments and kinetic as well as mutagenesis data, the structures of these formyl-CoA transferase complexes provide new information on the Class III CoA-transferase family and prompt redefinition of the catalytic steps and the modified reaction mechanism of formyl-CoA transferase proposed here.
About this StructureAbout this Structure
2VJO is a Single protein structure of sequence from Oxalobacter formigenes. Full crystallographic information is available from OCA.
ReferenceReference
Reinvestigation of the Catalytic Mechanism of Formyl-CoA Transferase, a Class III CoA-transferase., Berthold CL, Toyota CG, Richards NG, Lindqvist Y, J Biol Chem. 2008 Mar 7;283(10):6519-29. Epub 2007 Dec 27. PMID:18162462
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