We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1r0l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1r0l.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1r0l.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1r0l| PDB=1r0l | SCENE= }}
{{STRUCTURE_1r0l| PDB=1r0l | SCENE= }}
-
'''1-deoxy-D-xylulose 5-phosphate reductoisomerase from zymomonas mobilis in complex with NADPH'''
+
===1-deoxy-D-xylulose 5-phosphate reductoisomerase from zymomonas mobilis in complex with NADPH===
-
==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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15063313}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15063313 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15063313}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Reductoisomerase]]
[[Category: Reductoisomerase]]
[[Category: Zymomonas mobili]]
[[Category: Zymomonas mobili]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:55:35 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:06:16 2008''

Revision as of 10:06, 27 July 2008

Image:1r0l.png

Template:STRUCTURE 1r0l

1-deoxy-D-xylulose 5-phosphate reductoisomerase from zymomonas mobilis in complex with NADPH

Template:ABSTRACT PUBMED 15063313

About this Structure

1R0L 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 Sun Jul 27 13:06:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1r0l"
Personal tools