1u2d

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[[Image:1u2d.gif|left|200px]]
[[Image:1u2d.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1u2d |SIZE=350|CAPTION= <scene name='initialview01'>1u2d</scene>, resolution 3.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1u2d", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE= pntAA, nntA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1085 Rhodospirillum rubrum]), pntB, nntB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1085 Rhodospirillum rubrum])
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-->
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|DOMAIN=
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{{STRUCTURE_1u2d| PDB=1u2d | SCENE= }}
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|RELATEDENTRY=[[1hzz|1hzz]], [[1nm5|1nm5]], [[1ptj|1PTJ]], [[1u28|1u28]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u2d OCA], [http://www.ebi.ac.uk/pdbsum/1u2d PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u2d RCSB]</span>
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}}
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'''Structre of transhydrogenaes (dI.NADH)2(dIII.NADPH)1 asymmetric complex'''
'''Structre of transhydrogenaes (dI.NADH)2(dIII.NADPH)1 asymmetric complex'''
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==Reference==
==Reference==
Active-site conformational changes associated with hydride transfer in proton-translocating transhydrogenase., Mather OC, Singh A, van Boxel GI, White SA, Jackson JB, Biochemistry. 2004 Aug 31;43(34):10952-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15323555 15323555]
Active-site conformational changes associated with hydride transfer in proton-translocating transhydrogenase., Mather OC, Singh A, van Boxel GI, White SA, Jackson JB, Biochemistry. 2004 Aug 31;43(34):10952-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15323555 15323555]
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[[Category: NAD(P)(+) transhydrogenase (AB-specific)]]
 
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rhodospirillum rubrum]]
[[Category: Rhodospirillum rubrum]]
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[[Category: Singh, A.]]
[[Category: Singh, A.]]
[[Category: White, S A.]]
[[Category: White, S A.]]
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[[Category: nad(p) transhydrogenase subunit]]
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[[Category: Nad+]]
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[[Category: nad+]]
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[[Category: Nadp+]]
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[[Category: nadp+]]
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[[Category: Oxidoreductase]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:40:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:04:25 2008''
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Revision as of 07:40, 3 May 2008

Image:1u2d.gif

Template:STRUCTURE 1u2d

Structre of transhydrogenaes (dI.NADH)2(dIII.NADPH)1 asymmetric complex


Overview

Transhydrogenase couples the redox (hydride-transfer) reaction between NAD(H) and NADP(H) to proton translocation across a membrane. The redox reaction is catalyzed at the interface between two components (dI and dIII) which protrude from the membrane. A complex formed from recombinant dI and dIII (the dI(2)dIII(1) complex) from Rhodospirillum rubrum transhydrogenase catalyzes fast single-turnover hydride transfer between bound nucleotides. In this report we describe three new crystal structures of the dI(2)dIII(1) complex in different nucleotide-bound forms. The structures reveal an asymmetry in nucleotide binding that complements results from solution studies and supports the notion that intact transhydrogenase functions by an alternating site mechanism. In one structure, the redox site is occupied by NADH (on dI) and NADPH (on dIII). The dihydronicotinamide rings take up positions which may approximate to the ground state for hydride transfer: the redox-active C4(N) atoms are separated by only 3.6 A, and the perceived reaction stereochemistry matches that observed experimentally. The NADH conformation is different in the two dI polypeptides of this form of the dI(2)dIII(1) complex. Comparisons between a number of X-ray structures show that a conformational change in the NADH is driven by relative movement of the two domains which comprise dI. It is suggested that an equivalent conformational change in the intact enzyme is important in gating the hydride-transfer reaction. The observed nucleotide conformational change in the dI(2)dIII(1) complex is accompanied by rearrangements in the orientation of local amino acid side chains which may be responsible for sealing the site from the solvent and polarizing hydride transfer.

About this Structure

1U2D is a Protein complex structure of sequences from Rhodospirillum rubrum. Full crystallographic information is available from OCA.

Reference

Active-site conformational changes associated with hydride transfer in proton-translocating transhydrogenase., Mather OC, Singh A, van Boxel GI, White SA, Jackson JB, Biochemistry. 2004 Aug 31;43(34):10952-64. PMID:15323555 Page seeded by OCA on Sat May 3 10:40:12 2008

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