1x14: Difference between revisions
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> | |LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(AB-specific) NAD(P)(+) transhydrogenase (AB-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.2 1.6.1.2] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(P)(+)_transhydrogenase_(AB-specific) NAD(P)(+) transhydrogenase (AB-specific)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.1.2 1.6.1.2] </span> | ||
|GENE= pntA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= pntA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1x13|1X13]], [[1x15|1X15]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1x14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x14 OCA], [http://www.ebi.ac.uk/pdbsum/1x14 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1x14 RCSB]</span> | |||
}} | }} | ||
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[[Category: Rydstrom, J.]] | [[Category: Rydstrom, J.]] | ||
[[Category: Tornroth, S.]] | [[Category: Tornroth, S.]] | ||
[[Category: nad(h)-binding domain]] | [[Category: nad(h)-binding domain]] | ||
[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
[[Category: transhydrogenase]] | [[Category: transhydrogenase]] | ||
''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 00:43:31 2008'' | ||
Revision as of 00:43, 31 March 2008
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| , resolution 1.94Å | |||||||
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| Ligands: | |||||||
| Gene: | pntA (Escherichia coli) | ||||||
| Activity: | NAD(P)(+) transhydrogenase (AB-specific), with EC number 1.6.1.2 | ||||||
| Related: | 1X13, 1X15
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of E. coli transhydrogenase domain I with bound NAD
OverviewOverview
The dimeric integral membrane protein nicotinamide nucleotide transhydrogenase is required for cellular regeneration of NADPH in mitochondria and prokaryotes, for detoxification and biosynthesis purposes. Under physiological conditions, transhydrogenase couples the reversible reduction of NADP+ by NADH to an inward proton translocation across the membrane. Here, we present crystal structures of the NAD(H)-binding domain I of transhydrogenase from Escherichia coli, in the absence as well as in the presence of oxidized and reduced substrate. The structures were determined at 1.9-2.0 A resolution. Overall, the structures are highly similar to the crystal structure of a previously published NAD(H)-binding domain, from Rhodospirillum rubrum transhydrogenase. However, this particular domain is unique, since it is covalently connected to the integral-membrane part of transhydrogenase. Comparative studies between the structures of the two species reveal extensively differing surface properties and point to the possible importance of a rigid peptide (PAPP) in the connecting linker for conformational coupling. Further, the kinetic analysis of a deletion mutant, from which the protruding beta-hairpin was removed, indicates that this structural element is important for catalytic activity, but not for domain I:domain III interaction or dimer formation. Taken together, these results have important implications for the enzyme mechanism of the large group of transhydrogenases, including mammalian enzymes, which contain a connecting linker between domains I and II.
About this StructureAbout this Structure
1X14 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
X-ray structure of domain I of the proton-pumping membrane protein transhydrogenase from Escherichia coli., Johansson T, Oswald C, Pedersen A, Tornroth S, Okvist M, Karlsson BG, Rydstrom J, Krengel U, J Mol Biol. 2005 Sep 16;352(2):299-312. PMID:16083909
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