|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Crystal structure of the HypC-HypD-HypE complex (form II)== | | ==Crystal structure of the HypC-HypD-HypE complex (form II)== |
| - | <StructureSection load='3vyu' size='340' side='right' caption='[[3vyu]], [[Resolution|resolution]] 2.75Å' scene=''> | + | <StructureSection load='3vyu' size='340' side='right'caption='[[3vyu]], [[Resolution|resolution]] 2.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3vyu]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_kodakaraensis_(strain_kod1) Pyrococcus kodakaraensis (strain kod1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VYU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VYU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3vyu]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_kodakarensis_KOD1 Thermococcus kodakarensis KOD1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VYU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VYU 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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2z1c|2z1c]], [[2z1d|2z1d]], [[2z1e|2z1e]], [[3vyr|3vyr]], [[3vys|3vys]], [[3vyt|3vyt]]</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vyu OCA], [https://pdbe.org/3vyu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vyu RCSB], [https://www.ebi.ac.uk/pdbsum/3vyu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vyu ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tk-hypC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69014 Pyrococcus kodakaraensis (strain KOD1)]), Tk-hypD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69014 Pyrococcus kodakaraensis (strain KOD1)]), TK1993 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69014 Pyrococcus kodakaraensis (strain KOD1)])</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=3vyu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vyu OCA], [http://pdbe.org/3vyu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vyu RCSB], [http://www.ebi.ac.uk/pdbsum/3vyu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vyu ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q5JII0_THEKO Q5JII0_THEKO] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 20: |
Line 20: |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[HypA-HypB-HypC-HypD-HypE-HypF|HypA-HypB-HypC-HypD-HypE-HypF]] | + | *[[HypA%2C HypB%2C HypC%2C HypD%2C HypE and HypF 3D structures|HypA%2C HypB%2C HypC%2C HypD%2C HypE and HypF 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Miki, K]] | + | [[Category: Large Structures]] |
| - | [[Category: Watanabe, S]] | + | [[Category: Thermococcus kodakarensis KOD1]] |
| - | [[Category: Metal binding protein-transferase complex]] | + | [[Category: Miki K]] |
| | + | [[Category: Watanabe S]] |
| Structural highlights
Function
Q5JII0_THEKO
Publication Abstract from PubMed
[NiFe] hydrogenase maturation represents one of the most dynamic and sophisticated processes in metallocenter assembly. The Fe(CN)(2)CO moiety of [NiFe] hydrogenases is assembled via unknown transient interactions among specific maturation proteins HypC (metallochaperone), HypD (redox protein), and HypE (cyanide synthesis/donor). Here, we report the structures of the HypC-HypD and HypC-HypD-HypE complexes, providing a view of the transient interactions that take place during the maturation process. HypC binds to the conserved region of HypD through extensive hydrophobic interactions. The ternary complex formation between HypE and the HypCD complex involves both HypC and HypD, rendering the HypE conformation favorable for cyanide transfer. In the complex, the conserved cysteines of HypC and HypD form an Fe binding site. The conserved C-terminal cysteine of HypE can access the thiol redox cascade of HypD. These results provide structural insights into the Fe atom cyanation in the HypCDE complex.
Crystal Structures of the HypCD Complex and the HypCDE Ternary Complex: Transient Intermediate Complexes during [NiFe] Hydrogenase Maturation.,Watanabe S, Matsumi R, Atomi H, Imanaka T, Miki K Structure. 2012 Oct 30. pii: S0969-2126(12)00371-1. doi:, 10.1016/j.str.2012.09.018. PMID:23123111[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Watanabe S, Matsumi R, Atomi H, Imanaka T, Miki K. Crystal Structures of the HypCD Complex and the HypCDE Ternary Complex: Transient Intermediate Complexes during [NiFe] Hydrogenase Maturation. Structure. 2012 Oct 30. pii: S0969-2126(12)00371-1. doi:, 10.1016/j.str.2012.09.018. PMID:23123111 doi:10.1016/j.str.2012.09.018
|
