1mxs
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(New page: 200px<br /><applet load="1mxs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mxs, resolution 2.20Å" /> '''Crystal structure of...)
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Revision as of 19:40, 20 November 2007
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Crystal structure of 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase from Pseudomonas putida.
Overview
2-Keto-3-deoxy-6-phosphogluconate (KDPG) aldolase from Pseudomonas putida, is a key enzyme in the Entner-Doudoroff pathway which catalyses the, cleavage of KDPG via a class I Schiff-base mechanism. The crystal, structure of this enzyme has been refined to a crystallographic residual R, = 17.1% (R(free) = 21.4%). The N-terminal helix caps one side of the torus, of the (betaalpha)(8)-barrel and the active site is located on the, opposite, carboxylic side of the barrel. The Schiff-base-forming Lys145 is, coordinated by a sulfate (or phosphate) ion and two solvent water, molecules. The interactions that stabilize the trimer are predominantly, hydrophobic, with the exception of the cyclically permuted bonds formed, between Glu132 OE1 of one molecule and Thr129 OG1 of a symmetry-equivalent, molecule. Except for the N-terminal helix, the structure of KDPG aldolase, from P. putida closely resembles the structure of the homologous enzyme, from Escherichia coli.
About this Structure
1MXS is a Single protein structure of sequence from Pseudomonas putida with SO4 as ligand. Active as 2-dehydro-3-deoxy-phosphogluconate aldolase, with EC number 4.1.2.14 Full crystallographic information is available from OCA.
Reference
Structure of 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase from Pseudomonas putida., Bell BJ, Watanabe L, Rios-Steiner JL, Tulinsky A, Lebioda L, Arni RK, Acta Crystallogr D Biol Crystallogr. 2003 Aug;59(Pt 8):1454-8. Epub 2003, Jul 23. PMID:12876349
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