From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2q2v.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2q2v.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2q2v| PDB=2q2v | SCENE= }} | | {{STRUCTURE_2q2v| PDB=2q2v | SCENE= }} |
| | | | |
| - | '''Structure of D-3-Hydroxybutyrate Dehydrogenase from Pseudomonas putida'''
| + | ===Structure of D-3-Hydroxybutyrate Dehydrogenase from Pseudomonas putida=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17958702}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17958702 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_17958702}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 33: |
Line 37: |
| | [[Category: Pseudomonas putida]] | | [[Category: Pseudomonas putida]] |
| | [[Category: Sdr]] | | [[Category: Sdr]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:13:40 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:10:06 2008'' |
Revision as of 04:10, 28 July 2008
Template:STRUCTURE 2q2v
Structure of D-3-Hydroxybutyrate Dehydrogenase from Pseudomonas putida
Template:ABSTRACT PUBMED 17958702
About this Structure
2Q2V 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
Page seeded by OCA on Mon Jul 28 07:10:06 2008
