1sj2

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[[Image:1sj2.jpg|left|200px]]<br /><applet load="1sj2" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1sj2.jpg|left|200px]]
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caption="1sj2, resolution 2.41&Aring;" />
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'''Crystal structure of Mycobacterium tuberculosis catalase-peroxidase'''<br />
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{{Structure
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|PDB= 1sj2 |SIZE=350|CAPTION= <scene name='initialview01'>1sj2</scene>, resolution 2.41&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Catalase Catalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6]
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|GENE= KATG, RV1908C, MT1959, MTCY180.10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])
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}}
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'''Crystal structure of Mycobacterium tuberculosis catalase-peroxidase'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1SJ2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Catalase Catalase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.6 1.11.1.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SJ2 OCA].
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1SJ2 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=1SJ2 OCA].
==Reference==
==Reference==
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Crystal structure of Mycobacterium tuberculosis catalase-peroxidase., Bertrand T, Eady NA, Jones JN, Jesmin, Nagy JM, Jamart-Gregoire B, Raven EL, Brown KA, J Biol Chem. 2004 Sep 10;279(37):38991-9. Epub 2004 Jul 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15231843 15231843]
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Crystal structure of Mycobacterium tuberculosis catalase-peroxidase., Bertrand T, Eady NA, Jones JN, Jesmin, Nagy JM, Jamart-Gregoire B, Raven EL, Brown KA, J Biol Chem. 2004 Sep 10;279(37):38991-9. Epub 2004 Jul 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15231843 15231843]
[[Category: Catalase]]
[[Category: Catalase]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
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[[Category: homodimer]]
[[Category: homodimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:02:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:05:37 2008''

Revision as of 12:05, 20 March 2008


PDB ID 1sj2

Drag the structure with the mouse to rotate
, resolution 2.41Å
Ligands: and
Gene: KATG, RV1908C, MT1959, MTCY180.10 (Mycobacterium tuberculosis)
Activity: Catalase, with EC number 1.11.1.6
Coordinates: save as pdb, mmCIF, xml



Crystal structure of Mycobacterium tuberculosis catalase-peroxidase


Overview

The Mycobacterium tuberculosis catalase-peroxidase is a multifunctional heme-dependent enzyme that activates the core anti-tuberculosis drug isoniazid. Numerous studies have been undertaken to elucidate the enzyme-dependent mechanism of isoniazid activation, and it is well documented that mutations that reduce activity or inactivate the catalase-peroxidase lead to increased levels of isoniazid resistance in M. tuberculosis. Interpretation of the catalytic activities and the effects of mutations upon the action of the enzyme to date have been limited due to the lack of a three-dimensional structure for this enzyme. In order to provide a more accurate model of the three-dimensional structure of the M. tuberculosis catalase-peroxidase, we have crystallized the enzyme and now report its crystal structure refined to 2.4-A resolution. The structure reveals new information about dimer assembly and provides information about the location of residues that may play a role in catalysis including candidates for protein-based radical formation. Modeling and computational studies suggest that the binding site for isoniazid is located near the delta-meso heme edge rather than in a surface loop structure as currently proposed. The availability of a crystal structure for the M. tuberculosis catalase-peroxidase also permits structural and functional effects of mutations implicated in causing elevated levels of isoniazid resistance in clinical isolates to be interpreted with improved confidence.

About this Structure

1SJ2 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Crystal structure of Mycobacterium tuberculosis catalase-peroxidase., Bertrand T, Eady NA, Jones JN, Jesmin, Nagy JM, Jamart-Gregoire B, Raven EL, Brown KA, J Biol Chem. 2004 Sep 10;279(37):38991-9. Epub 2004 Jul 1. PMID:15231843

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