4g9i: Difference between revisions

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'''Unreleased structure'''


The entry 4g9i is ON HOLD
==Crystal structure of T.kodakarensis HypF==
<StructureSection load='4g9i' size='340' side='right'caption='[[4g9i]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4g9i]] is a 6 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=4G9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G9I FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=4g9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g9i OCA], [https://pdbe.org/4g9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g9i RCSB], [https://www.ebi.ac.uk/pdbsum/4g9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g9i ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5JII4_THEKO Q5JII4_THEKO]
<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.


Authors: Tominaga, T., Watanabe, S., Matsumi, R., Atomi, H., Imanaka, T., Miki, K.
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>


Description: Crystal structure of T.kodakarensis HypF
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4g9i" style="background-color:#fffaf0;"></div>
 
==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]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermococcus kodakarensis KOD1]]
[[Category: Atomi H]]
[[Category: Imanaka T]]
[[Category: Matsumi R]]
[[Category: Miki K]]
[[Category: Tominaga T]]
[[Category: Watanabe S]]