1xcb
From Proteopedia
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|GENE= rex ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=271 Thermus aquaticus]) | |GENE= rex ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=271 Thermus aquaticus]) | ||
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam02629 CoA_binding], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK05472 PRK05472], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam06971 Put_DNA-bind_N]</span> | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam02629 CoA_binding], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK05472 PRK05472], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam06971 Put_DNA-bind_N]</span> | ||
- | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xcb OCA], [http://www.ebi.ac.uk/pdbsum/1xcb PDBsum | + | |RELATEDENTRY= |
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xcb OCA], [http://www.ebi.ac.uk/pdbsum/1xcb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xcb RCSB]</span> | ||
}} | }} | ||
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[[Category: winged helix]] | [[Category: winged helix]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:47:40 2008'' |
Revision as of 21:47, 30 March 2008
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, resolution 2.9Å | |||||||
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Ligands: | , , | ||||||
Gene: | rex (Thermus aquaticus) | ||||||
Domains: | CoA_binding, PRK05472, Put_DNA-bind_N | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
X-ray Structure of a Rex-Family Repressor/NADH Complex from Thermus Aquaticus
Overview
The redox-sensing repressor Rex regulates transcription of respiratory genes in response to the intra cellular NADH/NAD(+) redox poise. As a step toward elucidating the molecular mechanism of NADH/NAD(+) sensing, the X-ray structure of Thermus aquaticus Rex (T-Rex) bound to effector NADH has been determined at 2.9 A resolution. The fold of the C-terminal domain of T-Rex is characteristic of NAD(H)-dependent enzymes, whereas the N-terminal domain is similar to a winged helix DNA binding motif. T-Rex dimerization is primarily mediated by "domain-swapped" alpha helices. Each NADH molecule binds to the C-terminal domain near the dimer interface. In contrast to NAD(H)-dependent enzymes, the nicotinamide is deeply buried within a hydrophobic pocket that appears to preclude substrate entry. We show that T-Rex binds to the Rex operator, and NADH but not NAD(+) inhibits T-Rex/DNA binding activity. A mechanism for redox sensing by Rex family members is proposed by analogy with domain closure of NAD(H)-dependent enzymes.
About this Structure
1XCB is a Single protein structure of sequence from Thermus aquaticus. This structure supersedes the now removed PDB entry 1R72. Full crystallographic information is available from OCA.
Reference
X-ray structure of a Rex-family repressor/NADH complex insights into the mechanism of redox sensing., Sickmier EA, Brekasis D, Paranawithana S, Bonanno JB, Paget MS, Burley SK, Kielkopf CL, Structure. 2005 Jan;13(1):43-54. PMID:15642260
Page seeded by OCA on Mon Mar 31 00:47:40 2008
Categories: Single protein | Thermus aquaticus | Bonanno, J B. | Brekasis, D. | Burley, S K. | Kielkopf, C L. | NYSGXRC, New York Structural GenomiX Research Consortium. | Paget, M S. | Paranawithana, S. | Sickmier, E A. | Nad | New york structural genomix research consortium | Nicotinamide adenine dinucleotide | Nysgxrc | Protein structure initiative | Psi | Redox-sensing | Rex | Rossmann fold | Structural genomic | Winged helix