2hji: Difference between revisions
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[[Image:2hji.gif|left|200px]]< | [[Image:2hji.gif|left|200px]] | ||
'''Structural model for the Fe-containing isoform of acireductone dioxygenase''' | {{Structure | ||
|PDB= 2hji |SIZE=350|CAPTION= <scene name='initialview01'>2hji</scene> | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=FE2:FE (II) ION'>FE2</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Acireductone_dioxygenase_(Fe(2+)-requiring) Acireductone dioxygenase (Fe(2+)-requiring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.54 1.13.11.54] | |||
|GENE= | |||
}} | |||
'''Structural model for the Fe-containing isoform of acireductone dioxygenase''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2HJI is a [ | 2HJI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Klebsiella_oxytoca Klebsiella oxytoca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HJI OCA]. | ||
==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:// | 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: Acireductone dioxygenase (Fe(2+)-requiring)]] | [[Category: Acireductone dioxygenase (Fe(2+)-requiring)]] | ||
[[Category: Klebsiella oxytoca]] | [[Category: Klebsiella oxytoca]] | ||
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[[Category: structural entropy]] | [[Category: structural entropy]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:17:50 2008'' | ||
Revision as of 15:17, 20 March 2008
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| Ligands: | FE2 | ||||||||||||
| Activity: | Acireductone dioxygenase (Fe(2+)-requiring), with EC number 1.13.11.54 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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