2c82: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:2c82.gif|left|200px]]
{{Seed}}
[[Image:2c82.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2c82|  PDB=2c82  |  SCENE=  }}  
{{STRUCTURE_2c82|  PDB=2c82  |  SCENE=  }}  


'''X-RAY STRUCTURE OF 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE, DXR, RV2870C, FROM MYCOBACTERIUM TUBERCULOSIS'''
===X-RAY STRUCTURE OF 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE, DXR, RV2870C, FROM MYCOBACTERIUM TUBERCULOSIS===




==Overview==
<!--  
1-deoxy-D-xylulose 5-phosphate reductoisomerase catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose 5-phosphate to form 2-C-methyl-D-erythritol 4-phosphate, as the second step of the deoxyxylulose 5-phosphate/methylerythritol 4-phosphate pathway found in many bacteria and plants. The end product, isopentenyl diphosphate, is the precursor of various isoprenoids vital to all living organisms. The pathway is not found in humans; the mevalonate pathway is instead used for the formation of isopentenyl diphosphate. This difference, combined with its essentiality, makes the reductoisomerase an excellent drug target in a number of pathogenic organisms. The structure of 1-deoxy-D-xylulose 5-phosphate reductoisomerase from Mycobacterium tuberculosis (Rv2870c) was solved by molecular replacement and refined to a resolution of 1.9 A. The enzyme exhibited an estimated kcat of 5.3 s-1 and Km and kcat/Km values of 7.2 microM and 7.4x10(5) M-1 s-1 for NADPH and 340 microM and 1.6x10(4) M-1 s-1 for 1-deoxy-D-xylulose 5-phosphate. In the structure, a sulfate is bound at the expected site of the phosphate moiety of the sugar substrate. The M. tuberculosis enzyme displays a similar fold to the previously published structures from Escherichia coli and Zymomonas mobilis. Comparisons offer suggestions for the design of specific drugs. Furthermore, the new structure represents an intermediate conformation between the open apo form and the closed holo form observed previously, giving insights into the conformational changes associated with catalysis.
The line below this paragraph, {{ABSTRACT_PUBMED_16790937}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 16790937 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_16790937}}


==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Rv2870c]]
[[Category: Rv2870c]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 21:25:31 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:07:19 2008''

Revision as of 15:07, 27 July 2008

File:2c82.png

Template:STRUCTURE 2c82

X-RAY STRUCTURE OF 1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE, DXR, RV2870C, FROM MYCOBACTERIUM TUBERCULOSIS

Template:ABSTRACT PUBMED 16790937

About this Structure

2C82 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

The 1.9 A resolution structure of Mycobacterium tuberculosis 1-deoxy-D-xylulose 5-phosphate reductoisomerase, a potential drug target., Henriksson LM, Bjorkelid C, Mowbray SL, Unge T, Acta Crystallogr D Biol Crystallogr. 2006 Jul;62(Pt 7):807-13. Epub 2006, Jun 20. PMID:16790937

Page seeded by OCA on Sun Jul 27 18:07:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2c82&oldid=659841"