1p9l: Difference between revisions

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[[Image:1p9l.gif|left|200px]]
{{Seed}}
[[Image:1p9l.png|left|200px]]


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{{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==
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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.
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{{ABSTRACT_PUBMED_12962488}}


==About this Structure==
==About this Structure==
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[[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

File: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

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