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5yy0

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Crystal structure of the HyhL-HypA complex (form II)

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Retrieved from "http://52.214.119.220/wiki/index.php/5yy0"

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 ==Crystal structure of the HyhL-HypA complex (form II)==
-<StructureSection load='5yy0' size='340' side='right' caption='[[5yy0]], [[Resolution|resolution]] 3.24&Aring;' scene=''>
+<StructureSection load='5yy0' size='340' side='right'caption='[[5yy0]], [[Resolution|resolution]] 3.24&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5yy0]] is a 2 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=5YY0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YY0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5yy0]] is a 2 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=5YY0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YY0 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 3.243&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hydA, TK2069 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69014 Pyrococcus kodakaraensis (strain KOD1)]), hypA, TK2008 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69014 Pyrococcus kodakaraensis (strain KOD1)])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5yy0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yy0 OCA], [http://pdbe.org/5yy0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yy0 RCSB], [http://www.ebi.ac.uk/pdbsum/5yy0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yy0 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=5yy0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yy0 OCA], [https://pdbe.org/5yy0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yy0 RCSB], [https://www.ebi.ac.uk/pdbsum/5yy0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yy0 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HYPA_THEKO HYPA_THEKO]] Probably plays a role in a hydrogenase nickel cofactor insertion step (By similarity).
+[https://www.uniprot.org/uniprot/Q8NKS2_THEKO Q8NKS2_THEKO]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Ni-Fe clusters are inserted into the large subunit of [NiFe] hydrogenases by maturation proteins such as the Ni chaperone HypA via an unknown mechanism. We determined crystal structures of an immature large subunit HyhL complexed with HypA from Thermococcus kodakarensis Structure analysis revealed that the N-terminal region of HyhL extends outwards and interacts with the Ni-binding domain of HypA. Intriguingly, the C-terminal extension of immature HyhL, which is cleaved in the mature form, adopts a beta-strand adjacent to its N-terminal beta-strands. The position of the C-terminal extension corresponds to that of the N-terminal extension of a mature large subunit, preventing the access of endopeptidases to the cleavage site of HyhL. These findings suggest that Ni insertion into the active site induces spatial rearrangement of both the N- and C-terminal tails of HyhL, which function as a key checkpoint for the completion of the Ni-Fe cluster assembly.
-Crystal structures of a [NiFe] hydrogenase large subunit HyhL in an immature state in complex with a Ni chaperone HypA.,Kwon S, Watanabe S, Nishitani Y, Kawashima T, Kanai T, Atomi H, Miki K Proc Natl Acad Sci U S A. 2018 Jul 3;115(27):7045-7050. doi:, 10.1073/pnas.1801955115. Epub 2018 Jun 18. PMID:29915046<ref>PMID:29915046</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5yy0" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Kwon, S]]
+[[Category: Large Structures]]
-[[Category: Miki, K]]
+[[Category: Thermococcus kodakarensis KOD1]]
-[[Category: Nishitani, Y]]
+[[Category: Kwon S]]
-[[Category: Watanabe, S]]
+[[Category: Miki K]]
-[[Category: Hydrogenase]]
+[[Category: Nishitani Y]]
-[[Category: Hyhl]]
+[[Category: Watanabe S]]
-[[Category: Hypa]]
-[[Category: Maturation]]
-[[Category: Metal binding protein]]

5yy0

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Crystal structure of the HyhL-HypA complex (form II)

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