2hji
From Proteopedia
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|PDB= 2hji |SIZE=350|CAPTION= <scene name='initialview01'>2hji</scene> | |PDB= 2hji |SIZE=350|CAPTION= <scene name='initialview01'>2hji</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FE2:FE (II) ION'>FE2</scene> | + | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1zrr|1ZRR]], [[1vr3|1VR3]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hji FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hji OCA], [http://www.ebi.ac.uk/pdbsum/2hji PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hji RCSB]</span> | ||
}} | }} | ||
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[[Category: Maroney, M J.]] | [[Category: Maroney, M J.]] | ||
[[Category: Pochapsky, T C.]] | [[Category: Pochapsky, T C.]] | ||
| - | [[Category: FE2]] | ||
[[Category: dioxygenase]] | [[Category: dioxygenase]] | ||
[[Category: isozyme]] | [[Category: isozyme]] | ||
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[[Category: structural entropy]] | [[Category: structural entropy]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:31:15 2008'' |
Revision as of 00:31, 31 March 2008
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| Ligands: | |||||||
| Activity: | Acireductone dioxygenase (Fe(2+)-requiring), with EC number 1.13.11.54 | ||||||
| Related: | 1ZRR, 1VR3
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Mon Mar 31 03:31:15 2008
