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1isu

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Revision as of 22:11, 10 September 2015

THE THREE-DIMENSIONAL STRUCTURE OF THE HIGH-POTENTIAL IRON-SULFUR PROTEIN ISOLATED FROM THE PURPLE PHOTOTROPHIC BACTERIUM RHODOCYCLUS TENUIS DETERMINED AND REFINED AT 1.5 ANGSTROMS RESOLUTION

Structural highlights

1isu is a 2 chain structure with sequence from Atcc 25093. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[HIP2_RHOTE] Specific class of high-redox-potential 4Fe-4S ferredoxins. Functions in anaerobic electron transport in most purple and in some other photosynthetic bacteria and in at least one genus (Paracoccus) of halophilic, denitrifying bacteria.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The molecular structure of the high-potential iron-sulfur protein (HiPIP) isolated from the phototrophic bacterium, Rhodocyclus tenuis, has been solved and refined to a nominal resolution of 1.5 A with a crystallographic R-factor of 17.3% for all measured X-ray data from 30 A to 1.5 A. It is the smallest of the HiPIP structures studied thus far with 62 amino acid residues. Crystals used in the investigation belonged to the space group P2(1) with unit cell dimensions of a = 36.7 A, b = 52.6 A, c = 27.6 A and beta = 90.8 degrees and contained two molecules per asymmetric unit. The structure was solved by a combination of multiple isomorphous replacement with two heavy-atom derivatives, anomalous scattering from the iron-sulfur cluster, symmetry averaging and solvent flattening. The folding motif for this HiPIP is characterized by one small alpha-helix, six Type I turns, an approximate Type II turn and one Type I' turn. As in other HiPIPs, the iron-sulfur cluster is co-ordinated by four cysteinyl ligands and exhibits a cubane-like motif. These cysteinyl ligands are all located in Type I turns. The hydrogen bonding around the metal cluster in the R. tenuis protein is similar to the patterns observed in the Chromatium vinosum and Ectothiorhodospira halophila HiPIPs. Several of the amino acid residues invariant in the previously determined C. vinosum and E. halophila structures are not retained in the R. tenuis molecule. There are 13 solvent molecules structurally conserved between the two R. tenuis HiPIP molecules in the asymmetric unit, some of which are important for stabilizing surface loops. Interestingly, while it is assumed that this HiPIP functions as a monomer in solution, the two molecules in the asymmetric unit pack as a dimer and are related to each other by an approximate twofold rotation axis.

Three-dimensional structure of the high-potential iron-sulfur protein isolated from the purple phototrophic bacterium Rhodocyclus tenuis determined and refined at 1.5 A resolution.,Rayment I, Wesenberg G, Meyer TE, Cusanovich MA, Holden HM J Mol Biol. 1992 Nov 20;228(2):672-86. PMID:1453470^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Rayment I, Wesenberg G, Meyer TE, Cusanovich MA, Holden HM. Three-dimensional structure of the high-potential iron-sulfur protein isolated from the purple phototrophic bacterium Rhodocyclus tenuis determined and refined at 1.5 A resolution. J Mol Biol. 1992 Nov 20;228(2):672-86. PMID:1453470

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1isu"

Categories: Atcc 25093 | Holden, H M

@@ Line 2: / Line 2: @@
 <StructureSection load='1isu' size='340' side='right' caption='[[1isu]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1isu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodocyclus_tenuis Rhodocyclus tenuis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ISU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ISU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1isu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25093 Atcc 25093]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ISU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ISU FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1isu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1isu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1isu RCSB], [http://www.ebi.ac.uk/pdbsum/1isu PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1isu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1isu OCA], [http://pdbe.org/1isu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1isu RCSB], [http://www.ebi.ac.uk/pdbsum/1isu PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1isu" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Rhodocyclus tenuis]]
+[[Category: Atcc 25093]]
 [[Category: Holden, H M]]

1isu

From Proteopedia

Revision as of 22:11, 10 September 2015

THE THREE-DIMENSIONAL STRUCTURE OF THE HIGH-POTENTIAL IRON-SULFUR PROTEIN ISOLATED FROM THE PURPLE PHOTOTROPHIC BACTERIUM RHODOCYCLUS TENUIS DETERMINED AND REFINED AT 1.5 ANGSTROMS RESOLUTION

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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