2hji: Difference between revisions
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'''Structural model for the Fe-containing isoform of acireductone dioxygenase''' | '''Structural model for the Fe-containing isoform of acireductone dioxygenase''' | ||
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==Reference== | ==Reference== | ||
One protein, two enzymes revisited: a structural entropy switch interconverts the two isoforms of acireductone dioxygenase., Ju T, Goldsmith RB, Chai SC, Maroney MJ, Pochapsky SS, Pochapsky TC, J Mol Biol. 2006 Nov 3;363(4):823-34. Epub 2006 Aug 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16989860 16989860] | One protein, two enzymes revisited: a structural entropy switch interconverts the two isoforms of acireductone dioxygenase., Ju T, Goldsmith RB, Chai SC, Maroney MJ, Pochapsky SS, Pochapsky TC, J Mol Biol. 2006 Nov 3;363(4):823-34. Epub 2006 Aug 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16989860 16989860] | ||
[[Category: Klebsiella oxytoca]] | [[Category: Klebsiella oxytoca]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Maroney, M J.]] | [[Category: Maroney, M J.]] | ||
[[Category: Pochapsky, T C.]] | [[Category: Pochapsky, T C.]] | ||
[[Category: | [[Category: Dioxygenase]] | ||
[[Category: | [[Category: Isozyme]] | ||
[[Category: | [[Category: Methionine salvage]] | ||
[[Category: | [[Category: Non-heme iron]] | ||
[[Category: | [[Category: Structural entropy]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:22:02 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 03:22, 4 May 2008
Structural model for the Fe-containing isoform of acireductone dioxygenase
Overview
Acireductone dioxygenase (ARD) catalyzes different reactions between O2 and 1,2-dihydroxy-3-oxo-5-(methylthio)pent-1-ene (acireductone) depending upon the metal bound in the active site. Ni2+ -ARD cleaves acireductone to formate, CO and methylthiopropionate. If Fe2+ is bound (ARD'), the same substrates yield methylthioketobutyrate and formate. The two forms differ in structure, and are chromatographically separable. Paramagnetism of Fe2+ renders the active site of ARD' inaccessible to standard NMR methods. The structure of ARD' has been determined using Fe2+ binding parameters determined by X-ray absorption spectroscopy and NMR restraints from H98S ARD, a metal-free diamagnetic protein that is isostructural with ARD'. ARD' retains the beta-sandwich fold of ARD, but a structural entropy switch increases order at one end of a two-helix system that bisects the beta-sandwich and decreases order at the other upon interconversion of ARD and ARD', causing loss of the C-terminal helix in ARD' and rearrangements of residues involved in substrate orientation in the active site.
About this Structure
2HJI is a Single protein structure of sequence from Klebsiella oxytoca. Full crystallographic information is available from OCA.
Reference
One protein, two enzymes revisited: a structural entropy switch interconverts the two isoforms of acireductone dioxygenase., Ju T, Goldsmith RB, Chai SC, Maroney MJ, Pochapsky SS, Pochapsky TC, J Mol Biol. 2006 Nov 3;363(4):823-34. Epub 2006 Aug 26. PMID:16989860 Page seeded by OCA on Sun May 4 06:22:02 2008
