HypA-HypB-HypC-HypD-HypE-HypF
From Proteopedia
(Difference between revisions)
Line 18: | Line 18: | ||
**[[4lps]] - HpHyp + GDP + Mg + Ni<br /> | **[[4lps]] - HpHyp + GDP + Mg + Ni<br /> | ||
+ | **[[2wsm]] – Hyp – ''Archaeoglobus fulgidus''<br /> | ||
*HypC | *HypC | ||
Line 40: | Line 41: | ||
**[[1gxt]], [[1gxu]] – EcHyp N terminal<br /> | **[[1gxt]], [[1gxu]] – EcHyp N terminal<br /> | ||
+ | **[[3tsp]] – EcHyp residues 92-746<br /> | ||
+ | **[[3tsq]] – EcHyp residues 92-746 + ATP + carbamoyl phosphate<br /> | ||
+ | **[[3ttc]] – EcHyp residues 92-746 + ADP + carbamoyl phosphate<br /> | ||
+ | **[[3ttf]] – EcHyp residues 92-746 + AMP + carbamoyl phosphate<br /> | ||
+ | **[[3tsu]] – EcHyp residues 92-746 + AMPPNP + carbamoyl phosphate<br /> | ||
+ | **[[3ttd]] – EcHyp residues 92-746 + AMPCPP + carbamoyl phosphate<br /> | ||
**[[4g9i]] - TkHyp <br /> | **[[4g9i]] - TkHyp <br /> | ||
Revision as of 10:05, 18 July 2018
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3D Structures of HypA, HypB, HypC, HypD, HypE and HypF
Updated on 18-July-2018
References
- ↑ Atanassova A, Zamble DB. Escherichia coli HypA is a zinc metalloprotein with a weak affinity for nickel. J Bacteriol. 2005 Jul;187(14):4689-97. PMID:15995183 doi:http://dx.doi.org/10.1128/JB.187.14.4689-4697.2005
- ↑ Olson JW, Fu C, Maier RJ. The HypB protein from Bradyrhizobium japonicum can store nickel and is required for the nickel-dependent transcriptional regulation of hydrogenase. Mol Microbiol. 1997 Apr;24(1):119-28. PMID:9140970
- ↑ Blokesch M, Paschos A, Bauer A, Reissmann S, Drapal N, Bock A. Analysis of the transcarbamoylation-dehydration reaction catalyzed by the hydrogenase maturation proteins HypF and HypE. Eur J Biochem. 2004 Aug;271(16):3428-36. PMID:15291820 doi:http://dx.doi.org/10.1111/j.1432-1033.2004.04280.x
- ↑ Blokesch M, Albracht SP, Matzanke BF, Drapal NM, Jacobi A, Bock A. The complex between hydrogenase-maturation proteins HypC and HypD is an intermediate in the supply of cyanide to the active site iron of [NiFe]-hydrogenases. J Mol Biol. 2004 Nov 12;344(1):155-67. PMID:15504408 doi:http://dx.doi.org/10.1016/j.jmb.2004.09.040