1c3v
From Proteopedia
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| - | [[Image:1c3v.gif|left|200px]] | + | [[Image:1c3v.gif|left|200px]] |
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| - | '''DIHYDRODIPICOLINATE REDUCTASE FROM MYCOBACTERIUM TUBERCULOSIS COMPLEXED WITH NADPH AND PDC''' | + | {{Structure |
| + | |PDB= 1c3v |SIZE=350|CAPTION= <scene name='initialview01'>1c3v</scene>, resolution 2.39Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=PDC:PYRIDINE-2,6-DICARBOXYLIC+ACID'>PDC</scene> and <scene name='pdbligand=PG4:TETRAETHYLENE GLYCOL'>PG4</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Dihydrodipicolinate_reductase Dihydrodipicolinate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.26 1.3.1.26] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''DIHYDRODIPICOLINATE REDUCTASE FROM MYCOBACTERIUM TUBERCULOSIS COMPLEXED WITH NADPH AND PDC''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1C3V is a [ | + | 1C3V is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C3V OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12962488 12962488] |
[[Category: Dihydrodipicolinate reductase]] | [[Category: Dihydrodipicolinate reductase]] | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
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[[Category: protein structure initiative]] | [[Category: protein structure initiative]] | ||
[[Category: psi]] | [[Category: psi]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
[[Category: tb structural genomics consortium]] | [[Category: tb structural genomics consortium]] | ||
[[Category: tbsgc]] | [[Category: tbsgc]] | ||
[[Category: two-domain structure]] | [[Category: two-domain structure]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:19:29 2008'' |
Revision as of 08:19, 20 March 2008
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| , resolution 2.39Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Activity: | Dihydrodipicolinate reductase, with EC number 1.3.1.26 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DIHYDRODIPICOLINATE REDUCTASE FROM MYCOBACTERIUM TUBERCULOSIS COMPLEXED WITH NADPH AND 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.
About this Structure
1C3V 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 Thu Mar 20 10:19:29 2008
Categories: Dihydrodipicolinate reductase | Mycobacterium tuberculosis | Single protein | Blanchard, J S. | Cirilli, M. | Scapin, G. | TBSGC, TB Structural Genomics Consortium. | Zheng, R. | NDP | PDC | PG4 | Protein structure initiative | Psi | Structural genomic | Tb structural genomics consortium | Tbsgc | Two-domain structure
