2z1e
From Proteopedia
(Difference between revisions)
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<StructureSection load='2z1e' size='340' side='right'caption='[[2z1e]], [[Resolution|resolution]] 1.55Å' scene=''> | <StructureSection load='2z1e' size='340' side='right'caption='[[2z1e]], [[Resolution|resolution]] 1.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2z1e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2z1e]] is a 1 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=2Z1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Z1E FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</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=2z1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z1e OCA], [https://pdbe.org/2z1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z1e RCSB], [https://www.ebi.ac.uk/pdbsum/2z1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z1e ProSAT]</span></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=2z1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2z1e OCA], [https://pdbe.org/2z1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2z1e RCSB], [https://www.ebi.ac.uk/pdbsum/2z1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2z1e ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q5JII7_THEKO Q5JII7_THEKO] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2z1e ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2z1e ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | [NiFe] hydrogenase maturation proteins HypC, HypD, and HypE catalyze the insertion and cyanation of the iron center of [NiFe] hydrogenases by an unknown mechanism. We have determined the crystal structures of HypC, HypD, and HypE from Thermococcus kodakaraensis KOD1 at 1.8 A, 2.07 A, and 1.55 A resolution, respectively. The structure of HypD reveals its probable iron binding and active sites for cyanation. An extended conformation of each conserved motif of HypC and HypE allows the essential cysteine residues of both proteins to interact with the active site of HypD. Furthermore, the C-terminal tail of HypE is shown to exist in an ATP-dependent dynamic equilibrium between outward and inward conformations. Unexpectedly, the [4Fe-4S] cluster environment of HypD is quite similar to that of ferredoxin:thioredoxin reductase (FTR), indicating the existence of a redox cascade similar to the FTR system. These results suggest a cyanation reaction mechanism via unique thiol redox signaling in the HypCDE complex. | ||
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| - | Crystal structures of [NiFe] hydrogenase maturation proteins HypC, HypD, and HypE: insights into cyanation reaction by thiol redox signaling.,Watanabe S, Matsumi R, Arai T, Atomi H, Imanaka T, Miki K Mol Cell. 2007 Jul 6;27(1):29-40. PMID:17612488<ref>PMID:17612488</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2z1e" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[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]] | *[[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/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Arai | + | [[Category: Thermococcus kodakarensis KOD1]] |
| - | [[Category: Atomi | + | [[Category: Arai T]] |
| - | [[Category: Imanaka | + | [[Category: Atomi H]] |
| - | [[Category: Matsumi | + | [[Category: Imanaka T]] |
| - | [[Category: Miki | + | [[Category: Matsumi R]] |
| - | [[Category: Watanabe | + | [[Category: Miki K]] |
| - | + | [[Category: Watanabe S]] | |
| - | + | ||
Current revision
Crystal structure of HypE from Thermococcus kodakaraensis (outward form)
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