1enz
From Proteopedia
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| - | [[Image:1enz.gif|left|200px]] | + | [[Image:1enz.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE AND FUNCTION OF THE ISONIAZID TARGET OF MYCOBACTERIUM TUBERCULOSIS''' | + | {{Structure |
| + | |PDB= 1enz |SIZE=350|CAPTION= <scene name='initialview01'>1enz</scene>, resolution 2.7Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE AND FUNCTION OF THE ISONIAZID TARGET OF MYCOBACTERIUM TUBERCULOSIS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ENZ is a [ | + | 1ENZ 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=1ENZ OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis., Dessen A, Quemard A, Blanchard JS, Jacobs WR Jr, Sacchettini JC, Science. 1995 Mar 17;267(5204):1638-41. PMID:[http:// | + | Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis., Dessen A, Quemard A, Blanchard JS, Jacobs WR Jr, Sacchettini JC, Science. 1995 Mar 17;267(5204):1638-41. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7886450 7886450] |
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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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]] | ||
| - | ''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 10:58:08 2008'' |
Revision as of 08:58, 20 March 2008
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| , resolution 2.7Å | |||||||
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| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE AND FUNCTION OF THE ISONIAZID TARGET OF MYCOBACTERIUM TUBERCULOSIS
Overview
Resistance to isoniazid in Mycobacterium tuberculosis can be mediated by substitution of alanine for serine 94 in the InhA protein, the drug's primary target. InhA was shown to catalyze the beta-nicotinamide adenine dinucleotide (NADH)-specific reduction of 2-trans-enoyl-acyl carrier protein, an essential step in fatty acid elongation. Kinetic analyses suggested that isoniazid resistance is due to a decreased affinity of the mutant protein for NADH. The three-dimensional structures of wild-type and mutant InhA, refined to 2.2 and 2.7 angstroms, respectively, revealed that drug resistance is directly related to a perturbation in the hydrogen-bonding network that stabilizes NADH binding.
About this Structure
1ENZ is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis., Dessen A, Quemard A, Blanchard JS, Jacobs WR Jr, Sacchettini JC, Science. 1995 Mar 17;267(5204):1638-41. PMID:7886450
Page seeded by OCA on Thu Mar 20 10:58:08 2008
