1a2i: Difference between revisions

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[[Image:1a2i.gif|left|200px]]
{{Seed}}
[[Image:1a2i.png|left|200px]]


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{{STRUCTURE_1a2i|  PDB=1a2i  |  SCENE=  }}  
{{STRUCTURE_1a2i|  PDB=1a2i  |  SCENE=  }}  


'''SOLUTION STRUCTURE OF DESULFOVIBRIO VULGARIS (HILDENBOROUGH) FERROCYTOCHROME C3, NMR, 20 STRUCTURES'''
===SOLUTION STRUCTURE OF DESULFOVIBRIO VULGARIS (HILDENBOROUGH) FERROCYTOCHROME C3, NMR, 20 STRUCTURES===




==Overview==
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Desulfovibrio vulgaris cytochrome c3 is a 14 kDa tetrahaem cytochrome that plays a central role in energy transduction. The three-dimensional structure of the ferrocytochrome at pH 8.5 was solved through two-dimensional 1H-NMR. The structures were calculated using a large amount of experimental information, which includes upper and lower distance limits as well as dihedral angle restraints. The analysis allows for fast-flipping aromatic residues and flexibility in the haem plane. The structure was determined using 2289 upper and 2390 lower distance limits, 63 restricted ranges for the phi torsion angle, 88 stereospecific assignments out of the 118 stereopairs with non-degenerate chemical shifts (74.6%), and 115 out of the 184 nuclear Overhauser effects to fast-flipping aromatic residues (62.5%), which were pseudo-stereospecifically assigned to one or the other side of the ring. The calculated NMR structures are very well defined, with an average root-mean-square deviation value relative to the mean coordinates of 0.35 A for the backbone atoms and 0.70 A for all heavy-atoms. Comparison of the NMR structures of the ferrocytochrome at pH 8.5 with the available X-ray structure of the ferricytochrome at pH 5.5 reveals that the general fold of the molecule is very similar, but that there are some distinct differences. Calculation of ring current shifts for the residues with significantly different conformations confirms that the NMR structures represent better its solution structure in the reduced form. Some of the localised differences, such as a reorientation of Thr24, are thought to be state-dependent changes that involve alterations in hydrogen bond networks. An important rearrangement in the vicinity of the propionate groups of haem I and involving the covalent linkage of haem II suggests that this is the critical region for the functional cooperativities of this protein.
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{{ABSTRACT_PUBMED_9710542}}


==About this Structure==
==About this Structure==
1A2I is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2I OCA].  
1A2I is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A2I OCA].  


==Reference==
==Reference==
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[[Category: Hemeprotein]]
[[Category: Hemeprotein]]
[[Category: Redox-bohr effect]]
[[Category: Redox-bohr effect]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:42:41 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:51:23 2008''

Revision as of 12:51, 30 June 2008

File:1a2i.png

Template:STRUCTURE 1a2i

SOLUTION STRUCTURE OF DESULFOVIBRIO VULGARIS (HILDENBOROUGH) FERROCYTOCHROME C3, NMR, 20 STRUCTURES

Template:ABSTRACT PUBMED 9710542

About this Structure

1A2I is a Single protein structure of sequence from Desulfovibrio vulgaris. Full experimental information is available from OCA.

Reference

Solution structure of Desulfovibrio vulgaris (Hildenborough) ferrocytochrome c3: structural basis for functional cooperativity., Messias AC, Kastrau DH, Costa HS, LeGall J, Turner DL, Santos H, Xavier AV, J Mol Biol. 1998 Aug 28;281(4):719-39. PMID:9710542

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