2i8l

<StructureSection load='2i8l' size='340' side='right'caption='[[2i8l]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[2i8l]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I8L OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2I8L FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2i8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i8l OCA], [http://pdbe.org/2i8l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2i8l RCSB], [http://www.ebi.ac.uk/pdbsum/2i8l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2i8l ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/HYCI_ECOLI HYCI_ECOLI]] Protease involved in the C-terminal processing of HycE, the large subunit of hydrogenase 3.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

[NiFe] hydrogenases are metalloenzymes involved in many biological processes concerning the metabolism of hydrogen. The maturation of the large subunit of these hydrogenases requires the cleavage of a peptide at the C terminus by an endopeptidase before the final formation of the [NiFe] metallocenter. HycI is an endopeptidase of the M52 family and responsible for the C-terminal cleavage of the large subunit of hydrogenase 3 in Escherichia coli. Although extensive studies were performed, the molecular mechanism of recognition and cleavage of hydrogenase 3 remains elusive. Herein, we report the solution structure of E. coli HycI determined by high resolution nuclear magnetic resonance spectroscopy. This is the first solution structure of the apo form of endopeptidase of the M52 family reported thus far. The overall structure is similar to the crystal structure of holo-HybD in the same family. However, significant diversity was observed between the two structures. Especially, HycI shows an open conformation at the putative nickel-binding site, whereas HybD adopts a closed conformation. In addition, we performed backbone dynamic studies to probe the motional properties of the apo form of HycI. Furthermore, the metal ion titration experiments provide insightful information on the substrate recognition and cleavage processes. Taken together, our current structural, biochemical, and dynamic studies extend the knowledge of the M52 family proteins and provide novel insights into the biological function of HycI.

Solution structure and backbone dynamics of an endopeptidase HycI from Escherichia coli: implications for mechanism of the [NiFe] hydrogenase maturation.,Yang F, Hu W, Xu H, Li C, Xia B, Jin C J Biol Chem. 2007 Feb 9;282(6):3856-63. Epub 2006 Dec 6. PMID:17150961<ref>PMID:17150961</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 2i8l" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillus coli migula 1895]]

[[Category: Hu, W]]

[[Category: Jin, C]]

[[Category: Yang, F]]

[[Category: Hydrolase]]