HypA-HypB-HypC-HypD-HypE-HypF
From Proteopedia
(Difference between revisions)
(New page: <StructureSection load='2z1d' size='340' side='right' caption='HypD with Fe4S4 center (PDB code 2z1d)' scene=''> The [NiFe] hydrogenase contains a NiFe(CO)(CN)2 in its reaction center...) |
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<StructureSection load='2z1d' size='340' side='right' caption='HypD with Fe4S4 center (PDB code [[2z1d]])' scene=''> | <StructureSection load='2z1d' size='340' side='right' caption='HypD with Fe4S4 center (PDB code [[2z1d]])' scene=''> | ||
- | The [NiFe] hydrogenase contains a NiFe(CO)(CN)2 in its reaction center. '''HypA, HypB, HypC, HypD, HypE and HypF''' are required for the maturation of [NiFe] hydrogenase. '''HypA''' and '''HypB''' are involved in the insertion of Ni atom. '''HypE''' and '''HypF''' catalyze the biosynthesis of the CN ligand. '''HypC''' and '''HypD''' deliver the Fe and CO to the hydrogenase active center. For more details of HypA see [[Molecular Playground/HypA]]. | ||
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== Function == | == Function == | ||
+ | The [NiFe] hydrogenase or '''hydrogenase expression/formation protein''' contains a NiFe(CO)(CN)2 in its reaction center. '''HypA, HypB, HypC, HypD, HypE and HypF''' are required for the maturation of [NiFe] hydrogenase. | ||
+ | *'''HypA'''<ref>PMID:15995183</ref> and '''HypB'''<ref>PMID:9140970</ref> are involved in the insertion of Ni atom. For more details of HypA see [[Molecular Playground/HypA]]. | ||
+ | *'''HypE''' and '''HypF'''<ref>PMID:15291820</ref> catalyze the biosynthesis of the CN ligand. | ||
+ | *'''HypC''' and '''HypD'''<ref>PMID:15504408</ref> deliver the Fe and CO to the hydrogenase active center. | ||
- | == | + | == 3D Structures of HypA, HypB, HypC, HypD, HypE and HypF == |
- | + | [[HypA, HypB, HypC, HypD, HypE and HypF 3D structures]] | |
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</StructureSection> | </StructureSection> | ||
- | == 3D Structures of HypA, HypB, HypC, HypD, HypE and HypF == | ||
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- | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
- | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
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- | *HypA | ||
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- | **[[3a43]] - EcHyp - ''Escherichia coli''<br /> | ||
- | **[[3a44]] - PkHyp - ''Pyrococcus kodakaraensis''<br /> | ||
- | **[[2kdx]] - HpHyp - ''Helicobacter pylori'' - NMR<br /> | ||
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- | *HypB | ||
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- | **[[4lps]] - HpHyp + GDP + Mg + Ni<br /> | ||
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- | *HypC | ||
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- | **[[2z1c]] - TkHyp - ''Thermococcus kodakaraensis''<br /> | ||
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- | *HypD | ||
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- | **[[2z1d]] - TkHyp + Fe4S4<br /> | ||
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- | *HypE | ||
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- | **[[2z1e]], [[2z1f]] - PkHyp<br /> | ||
- | **[[3wjp]] - TkHyp + carbamoyl-CN + Mg <br /> | ||
- | **[[3wjq]] - TkHyp + Cys-CN + Mg <br /> | ||
- | **[[3wjr]] - TkHyp + AMP + Mg <br /> | ||
- | **[[2z1t]] – DvHyp – ''Desulfovibrio vulgaris''<br /> | ||
- | **[[2z1u]] – DvHyp + ATP<br /> | ||
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- | *HypF | ||
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- | **[[1gxt]], [[1gxu]] – EcHyp N terminal<br /> | ||
- | **[[4g9i]] - TkHyp <br /> | ||
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- | *HypC-HypD | ||
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- | **[[3vyr]] - TkHyp + Fe4S4 <br /> | ||
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- | *HypC-HypD-HypE | ||
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- | **[[3vys]], [[3vyt]], [[3vyu]] - TkHyp + Fe4S4 + Mg <br /> | ||
- | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
+ | [[Category:Topic Page]] |
Current revision
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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