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1hrq

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Revision as of 10:24, 30 October 2019

THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE REDUCED HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM VINOSUM THROUGH NMR

Structural highlights

1hrq is a 1 chain structure with sequence from "bacillus_vinosus"_(ehrenberg_1838)_trevisan_1889 "bacillus vinosus" (ehrenberg 1838) trevisan 1889. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HIP_ALLVD] 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 1H NMR assignment of the reduced HiPIP from Chromatium vinosum available in the literature [Gaillard, J., Albrand, J.-P., Moulis, J.-M., & Wemmer, D. E. (1992) Biochemistry 31, 5632-5639] has been extended up to 85% of the total protein protons. Ninety percent of the nitrogens have been assigned. Then the solution structure has been obtained using as many as 1147 meaningful NOE connectivities. The protein is sizably paramagnetic even though the ground state is a singlet. Nevertheless, the final RMSD values are 0.62 and 1.19 A for the backbone and the heavy atoms, respectively. These values compare well with those for diamagnetic proteins of the same size. The solution structure is discussed in the light of the available structural information from X-ray data.

The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR.,Banci L, Bertini I, Dikiy A, Kastrau DH, Luchinat C, Sompornpisut P Biochemistry. 1995 Jan 10;34(1):206-19. PMID:7819198^[1]

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

References

↑ Banci L, Bertini I, Dikiy A, Kastrau DH, Luchinat C, Sompornpisut P. The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR. Biochemistry. 1995 Jan 10;34(1):206-19. PMID:7819198

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/1hrq"

@@ Line 1: / Line 1: @@
 ==THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE REDUCED HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM VINOSUM THROUGH NMR==
-<StructureSection load='1hrq' size='340' side='right' caption='[[1hrq]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
+<StructureSection load='1hrq' size='340' side='right'caption='[[1hrq]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1hrq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_vinosus"_(ehrenberg_1838)_trevisan_1889 "bacillus vinosus" (ehrenberg 1838) trevisan 1889]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HRQ FirstGlance]. <br>
@@ Line 32: / Line 32: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Banci, L]]
 [[Category: Bertini, I]]

1hrq

From Proteopedia

Revision as of 10:24, 30 October 2019

THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE REDUCED HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM VINOSUM THROUGH NMR

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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