This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1p9l

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1p9l.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1p9l.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1p9l| PDB=1p9l | SCENE= }}
{{STRUCTURE_1p9l| PDB=1p9l | SCENE= }}
-
'''Structure of M. tuberculosis dihydrodipicolinate reductase in complex with NADH and 2,6 PDC'''
+
===Structure of M. tuberculosis dihydrodipicolinate reductase in complex with NADH and 2,6 PDC===
-
==Overview==
+
<!--
-
Dihydrodipicolinate reductase (DHPR) catalyzes the reduced pyridine nucleotide-dependent reduction of the alpha,beta-unsaturated cyclic imine, dihydrodipicolinate, to generate tetrahydrodipicolinate. This enzyme catalyzes the second step in the bacterial biosynthetic pathway that generates meso-diaminopimelate, a component of bacterial cell walls, and the amino acid L-lysine. The Mycobacterium tuberculosis dapB-encoded DHPR has been cloned, expressed, purified, and crystallized in two ternary complexes with NADH or NADPH and the inhibitor 2,6-pyridinedicarboxylate (2,6-PDC). The structures have been solved using molecular replacement strategies, and the DHPR-NADH-2,6-PDC and DHPR-NADPH-2,6-PDC complexes have been refined against data to 2.3 and 2.5 A, respectively. The M. tuberculosis DHPR is a tetramer of identical subunits, with each subunit composed of two domains connected by two flexible hinge regions. The N-terminal domain binds pyridine nucleotide, while the C-terminal domain is involved in both tetramer formation and substrate/inhibitor binding. The M. tuberculosis DHPR uses NADH and NADPH with nearly equal efficiency based on V/K values. To probe the nature of this substrate specificity, we have generated two mutants, K9A and K11A, residues that are close to the 2'-phosphate of NADPH. These two mutants exhibit decreased specificity for NADPH by factors of 6- and 30-fold, respectively, but the K11A mutant exhibits 270% of WT activity using NADH. The highly conserved structure of the nucleotide fold may permit other enzyme's nucleotide specificity to be altered using similar mutagenic strategies.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12962488}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12962488 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12962488}}
==About this Structure==
==About this Structure==
Line 37: Line 41:
[[Category: Tb structural genomics consortium]]
[[Category: Tb structural genomics consortium]]
[[Category: Tbsgc]]
[[Category: Tbsgc]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:51:14 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:28:41 2008''

Revision as of 10:28, 29 July 2008

Image:1p9l.png

Template:STRUCTURE 1p9l

Structure of M. tuberculosis dihydrodipicolinate reductase in complex with NADH and 2,6 PDC

Template:ABSTRACT PUBMED 12962488

About this Structure

1P9L is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

The three-dimensional structures of the Mycobacterium tuberculosis dihydrodipicolinate reductase-NADH-2,6-PDC and -NADPH-2,6-PDC complexes. Structural and mutagenic analysis of relaxed nucleotide specificity., Cirilli M, Zheng R, Scapin G, Blanchard JS, Biochemistry. 2003 Sep 16;42(36):10644-50. PMID:12962488

Page seeded by OCA on Tue Jul 29 13:28:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1p9l"
Personal tools