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1hlq

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Revision as of 16:15, 25 December 2014

CRYSTAL STRUCTURE OF RHODOFERAX FERMENTANS HIGH POTENTIAL IRON-SULFUR PROTEIN REFINED TO 1.45 A

Structural highlights

1hlq is a 3 chain structure with sequence from Rhodoferax fermentans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[HIP_RHOFE] 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. Competent in photosynthetic electron transfer to oxidized cytochrome bc1 complex via the membrane-bound c-type tetraheme.^[1] [:]^[2] ^[3] ^[4] ^[5]

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 crystal structure of Rhodoferax fermentans high-potential iron protein (HiPIP) has been solved by MAD methods using the anomalous signal from the Fe atoms in the [Fe(4)S(4)] cluster present in the protein and refined to a resolution of 1.45 A. The peptide chain is well defined except in the N- and C-terminal areas. The structure of the protein reveals the presence of three helical fragments, a small beta-sheet and several turns, with the [Fe(4)S(4)] cluster being located close to a surface patch containing several well conserved aromatic residues. The protein fold is very similar to the structures of other known HiPIPs, especially in the region proximal to the [Fe(4)S(4)] cluster, while the largest differences are observed on the opposite side of the protein, which is rich in positive charges and has no sequential homology to other HiPIP families.

Structure of Rhodoferax fermentans high-potential iron-sulfur protein solved by MAD.,Gonzalez A, Benini S, Ciurli S Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1582-8. Epub 2003, Aug 19. PMID:12925788^[6]

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

References

↑ Hochkoeppler A, Kofod P, Ferro G, Ciurli S. Isolation, characterization, and functional role of the high-potential iron-sulfur protein (HiPIP) from Rhodoferax fermentans. Arch Biochem Biophys. 1995 Oct 1;322(2):313-8. PMID:7574702 doi:http://dx.doi.org/10.1006/abbi.1995.1469
↑ Hochkoeppler A, Ciurli S, Venturoli G, Zannoni D. The high potential iron-sulfur protein (HiPIP) from Rhodoferax fermentans is competent in photosynthetic electron transfer. FEBS Lett. 1995 Jan 2;357(1):70-4. PMID:8001683
↑ Hochkoeppler A, Kofod P, Zannoni D. HiPiP oxido-reductase activity in membranes from aerobically grown cells of the facultative phototroph Rhodoferax fermentans. FEBS Lett. 1995 Nov 20;375(3):197-200. PMID:7498498
↑ Hochkoeppler A, Zannoni D, Ciurli S, Meyer TE, Cusanovich MA, Tollin G. Kinetics of photo-induced electron transfer from high-potential iron-sulfur protein to the photosynthetic reaction center of the purple phototroph Rhodoferax fermentans. Proc Natl Acad Sci U S A. 1996 Jul 9;93(14):6998-7002. PMID:8692932
↑ Bonora P, Principi I I, Monti B, Ciurli S, Zannoni D, Hochkoeppler A. On the role of high-potential iron-sulfur proteins and cytochromes in the respiratory chain of two facultative phototrophs Biochim Biophys Acta. 1999 Jan 27;1410(1):51-60. PMID:10076014
↑ Gonzalez A, Benini S, Ciurli S. Structure of Rhodoferax fermentans high-potential iron-sulfur protein solved by MAD. Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1582-8. Epub 2003, Aug 19. PMID:12925788

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/1hlq"

@@ Line 6: / Line 6: @@
 <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=1hlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hlq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1hlq RCSB], [http://www.ebi.ac.uk/pdbsum/1hlq PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/HIP_RHOFE HIP_RHOFE]] 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. Competent in photosynthetic electron transfer to oxidized cytochrome bc1 complex via the membrane-bound c-type tetraheme.<ref>PMID:7574702</ref> [:]<ref>PMID:8001683</ref> <ref>PMID:7498498</ref> <ref>PMID:8692932</ref> <ref>PMID:10076014</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1hlq

From Proteopedia

Revision as of 16:15, 25 December 2014

CRYSTAL STRUCTURE OF RHODOFERAX FERMENTANS HIGH POTENTIAL IRON-SULFUR PROTEIN REFINED TO 1.45 A

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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