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4g9i
From Proteopedia
(Difference between revisions)
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| - | [[ | + | ==Crystal structure of T.kodakarensis HypF== |
| + | <StructureSection load='4g9i' size='340' side='right' caption='[[4g9i]], [[Resolution|resolution]] 4.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4g9i]] is a 6 chain structure with sequence from [http://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=4G9I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G9I 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> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hypF, TK1997 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=69014 Thermococcus kodakarensis 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=4g9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g9i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g9i RCSB], [http://www.ebi.ac.uk/pdbsum/4g9i PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | HypF is involved in the biosynthesis of the CN ligand of the NiFe(CN)(2)CO centre of [NiFe]-hydrogenases. Here, the full-length structure of HypF from Thermococcus kodakarenesis is reported at 4.5 A resolution. The N-terminal acylphosphatase-like (ACP) domain interacts with the zinc-finger domain with some flexibility in its relative position. Molecular-surface analysis shows that a deep pocket formed between the ACP and zinc-finger domains is highly conserved and has positive potential. These results suggest that the positively charged pocket identified is involved in the hydrolysis of carbamoyl phosphate and the formation of a carbamoyl intermediate. | ||
| - | + | Structure of the [NiFe]-hydrogenase maturation protein HypF from Thermococcus kodakarensis KOD1.,Tominaga T, Watanabe S, Matsumi R, Atomi H, Imanaka T, Miki K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Oct 1;68(Pt 10):1153-7., doi: 10.1107/S1744309112036421. Epub 2012 Sep 22. PMID:23027738<ref>PMID:23027738</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Thermococcus kodakarensis kod1]] | [[Category: Thermococcus kodakarensis kod1]] | ||
| - | [[Category: Atomi, H | + | [[Category: Atomi, H]] |
| - | [[Category: Imanaka, T | + | [[Category: Imanaka, T]] |
| - | [[Category: Matsumi, R | + | [[Category: Matsumi, R]] |
| - | [[Category: Miki, K | + | [[Category: Miki, K]] |
| - | [[Category: Tominaga, T | + | [[Category: Tominaga, T]] |
| - | [[Category: Watanabe, S | + | [[Category: Watanabe, S]] |
[[Category: Atp binding]] | [[Category: Atp binding]] | ||
[[Category: Carbamoylation]] | [[Category: Carbamoylation]] | ||
Revision as of 09:23, 10 December 2014
Crystal structure of T.kodakarensis HypF
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