2a87: Difference between revisions
New page: left|200px<br /><applet load="2a87" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a87, resolution 3.00Å" /> '''Crystal Structure of... |
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[[Image:2a87.gif|left|200px]]<br /><applet load="2a87" size=" | [[Image:2a87.gif|left|200px]]<br /><applet load="2a87" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2a87, resolution 3.00Å" /> | caption="2a87, resolution 3.00Å" /> | ||
'''Crystal Structure of M. tuberculosis Thioredoxin reductase'''<br /> | '''Crystal Structure of M. tuberculosis Thioredoxin reductase'''<br /> | ||
==Overview== | ==Overview== | ||
The thioredoxin system exists ubiquitously and participates in essential | The thioredoxin system exists ubiquitously and participates in essential antioxidant and redox-regulation processes via a pair of conserved cysteine residues. In Mycobacterium tuberculosis, which lacks a genuine glutathione system, the thioredoxin system provides reducing equivalents inside the cell. The three-dimensional structure of thioredoxin reductase from M. tuberculosis has been determined at 3 A resolution. TLS refinement reveals a large libration axis, showing that NADPH-binding domain has large anisotropic disorder. The relative rotation of the NADPH domain with respect to the FAD domain is necessary for the thioredoxin reduction cycle, as it brings the spatially distant reacting sites close together. Normal-mode analysis carried out based on the elastic network model shows that the motion required to bring about the functional conformational change can be accounted for by motion along one single mode. TLS refinement and normal-mode analysis thus enhance our understanding of the associated conformational changes. | ||
==About this Structure== | ==About this Structure== | ||
2A87 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 MG, FAD and NAP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] Full crystallographic information is available from [http:// | 2A87 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=MG:'>MG</scene>, <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=NAP:'>NAP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Thioredoxin-disulfide_reductase Thioredoxin-disulfide reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.9 1.8.1.9] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A87 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Thioredoxin-disulfide reductase]] | [[Category: Thioredoxin-disulfide reductase]] | ||
[[Category: Akif, M.]] | [[Category: Akif, M.]] | ||
[[Category: Mande, S | [[Category: Mande, S C.]] | ||
[[Category: Suhre, K.]] | [[Category: Suhre, K.]] | ||
[[Category: TBSGC, TB | [[Category: TBSGC, TB Structural Genomics Consortium.]] | ||
[[Category: Verma, C.]] | [[Category: Verma, C.]] | ||
[[Category: FAD]] | [[Category: FAD]] | ||
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[[Category: trxr]] | [[Category: trxr]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:24:32 2008'' | ||
Revision as of 17:24, 21 February 2008
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Crystal Structure of M. tuberculosis Thioredoxin reductase
OverviewOverview
The thioredoxin system exists ubiquitously and participates in essential antioxidant and redox-regulation processes via a pair of conserved cysteine residues. In Mycobacterium tuberculosis, which lacks a genuine glutathione system, the thioredoxin system provides reducing equivalents inside the cell. The three-dimensional structure of thioredoxin reductase from M. tuberculosis has been determined at 3 A resolution. TLS refinement reveals a large libration axis, showing that NADPH-binding domain has large anisotropic disorder. The relative rotation of the NADPH domain with respect to the FAD domain is necessary for the thioredoxin reduction cycle, as it brings the spatially distant reacting sites close together. Normal-mode analysis carried out based on the elastic network model shows that the motion required to bring about the functional conformational change can be accounted for by motion along one single mode. TLS refinement and normal-mode analysis thus enhance our understanding of the associated conformational changes.
About this StructureAbout this Structure
2A87 is a Single protein structure of sequence from Mycobacterium tuberculosis with , and as ligands. Active as Thioredoxin-disulfide reductase, with EC number 1.8.1.9 Full crystallographic information is available from OCA.
ReferenceReference
Conformational flexibility of Mycobacterium tuberculosis thioredoxin reductase: crystal structure and normal-mode analysis., Akif M, Suhre K, Verma C, Mande SC, Acta Crystallogr D Biol Crystallogr. 2005 Dec;61(Pt 12):1603-11. Epub 2005, Nov 19. PMID:16301794
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Mycobacterium tuberculosis
- Single protein
- Thioredoxin-disulfide reductase
- Akif, M.
- Mande, S C.
- Suhre, K.
- TBSGC, TB Structural Genomics Consortium.
- Verma, C.
- FAD
- MG
- NAP
- Fad
- Nap
- Nma
- Oxidoreductase
- Protein structure initiative
- Psi
- Structural genomics
- Tb structural genomics consortium
- Tbsgc
- Thioredoxin reductase
- Tls
- Trxr