1r0k
From Proteopedia
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'''Crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase from Zymomonas mobilis''' | '''Crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase from Zymomonas mobilis''' | ||
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[[Category: Sahm, H.]] | [[Category: Sahm, H.]] | ||
[[Category: Schneider, G.]] | [[Category: Schneider, G.]] | ||
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| - | [[Category: | + | [[Category: Nadph dependent]] |
| - | [[Category: | + | [[Category: Non-mevalonate pathway]] |
| - | [[Category: | + | [[Category: Reductoisomerase]] |
| - | [[Category: | + | [[Category: Zymomonas mobili]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:55:34 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:55, 3 May 2008
Crystal structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase from Zymomonas mobilis
Overview
1-Deoxy-d-xylulose-5-phosphate reductoisomerase (DXR) is the second enzyme in the non-mevalonate pathway of isoprenoid biosynthesis. The structure of the apo-form of this enzyme from Zymomonas mobilis has been solved and refined to 1.9-A resolution, and that of a binary complex with the co-substrate NADPH to 2.7-A resolution. The subunit of DXR consists of three domains. Residues 1-150 form the NADPH binding domain, which is a variant of the typical dinucleotide-binding fold. The second domain comprises a four-stranded mixed beta-sheet, with three helices flanking the sheet. Most of the putative active site residues are located on this domain. The C-terminal domain (residues 300-386) folds into a four-helix bundle. In solution and in the crystal, the enzyme forms a homo-dimer. The interface between the two monomers is formed predominantly by extension of the sheet in the second domain. The adenosine phosphate moiety of NADPH binds to the nucleotide-binding fold in the canonical way. The adenine ring interacts with the loop after beta1 and with the loops between alpha2 and beta2 and alpha5 and beta5. The nicotinamide ring is disordered in crystals of this binary complex. Comparisons to Escherichia coli DXR show that the two enzymes are very similar in structure, and that the active site architecture is highly conserved. However, there are differences in the recognition of the adenine ring of NADPH in the two enzymes.
About this Structure
1R0K is a Single protein structure of sequence from Zymomonas mobilis. Full crystallographic information is available from OCA.
Reference
Crystal structure of 1-deoxy-d-xylulose-5-phosphate reductoisomerase from Zymomonas mobilis at 1.9-A resolution., Ricagno S, Grolle S, Bringer-Meyer S, Sahm H, Lindqvist Y, Schneider G, Biochim Biophys Acta. 2004 Apr 8;1698(1):37-44. PMID:15063313 Page seeded by OCA on Sat May 3 06:55:34 2008
