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2q2w

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[[Image:2q2w.gif|left|200px]]
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{{STRUCTURE_2q2w| PDB=2q2w | SCENE= }}
{{STRUCTURE_2q2w| PDB=2q2w | SCENE= }}
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'''Structure of D-3-Hydroxybutyrate Dehydrogenase from Pseudomonas putida'''
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===Structure of D-3-Hydroxybutyrate Dehydrogenase from Pseudomonas putida===
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==Overview==
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D-3-Hydroxybutyrate dehydrogenase from Pseudomonas putida belongs to the family of short-chain dehydrogenases/reductases. We have determined X-ray structures of the D-3-hydroxybutyrate dehydrogenase from Pseudomonas putida, which was recombinantly expressed in Escherichia coli, in three different crystal forms to resolutions between 1.9 and 2.1 A. The so-called substrate-binding loop (residues 187-210) was partially disordered in several subunits, in both the presence and absence of NAD(+). However, in two subunits, this loop was completely defined in an open conformation in the apoenzyme and in a closed conformation in the complex structure with NAD(+). Structural comparisons indicated that the loop moves as a rigid body by about 46 degrees . However, the two small alpha-helices (alphaFG1 and alphaFG2) of the loop also re-orientated slightly during the conformational change. Probably, the interactions of Val185, Thr187 and Leu189 with the cosubstrate induced the conformational change. A model of the binding mode of the substrate D-3-hydroxybutyrate indicated that the loop in the closed conformation, as a result of NAD(+) binding, is positioned competent for catalysis. Gln193 is the only residue of the substrate-binding loop that interacts directly with the substrate. A translation, libration and screw (TLS) analysis of the rigid body movement of the loop in the crystal showed significant librational displacements, describing the coordinated movement of the substrate-binding loop in the crystal. NAD(+) binding increased the flexibility of the substrate-binding loop and shifted the equilibrium between the open and closed forms towards the closed form. The finding that all NAD(+) -bound subunits are present in the closed form and all NAD(+) -free subunits in the open form indicates that the loop closure is induced by cosubstrate binding alone. This mechanism may contribute to the sequential binding of cosubstrate followed by substrate.
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{{ABSTRACT_PUBMED_17958702}}
==About this Structure==
==About this Structure==
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[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:13:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:42:46 2008''

Revision as of 16:42, 27 July 2008

Image:2q2w.png

Template:STRUCTURE 2q2w

Structure of D-3-Hydroxybutyrate Dehydrogenase from Pseudomonas putida

Template:ABSTRACT PUBMED 17958702

About this Structure

2Q2W is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.

Reference

Cosubstrate-induced dynamics of D-3-hydroxybutyrate dehydrogenase from Pseudomonas putida., Paithankar KS, Feller C, Kuettner EB, Keim A, Grunow M, Strater N, FEBS J. 2007 Nov;274(21):5767-79. PMID:17958702

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