View source for 4i52


==scMenB im complex with 1-hydroxy-2-naphthoyl-CoA==
<StructureSection load='4i52' size='340' side='right'caption='[[4i52]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4i52]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803_substr._Kazusa Synechocystis sp. PCC 6803 substr. Kazusa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I52 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1HA:1-HYDROXY-2-NAPHTHOYL-COA'>1HA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=4i52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i52 OCA], [https://pdbe.org/4i52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i52 RCSB], [https://www.ebi.ac.uk/pdbsum/4i52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i52 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/P73495_SYNY3 P73495_SYNY3] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
1, 4-Dihydroxy-2-naphthoyl coenzyme A (DHNA-CoA) synthase is a typical crotonase fold enzyme with an implicated role of conformational changes in catalysis. We have identified these conformational changes by determining the structures of its Escherichia coli and Synechocystis sp. PCC6803 orthologues in complex with a product analog. The structural changes include the folding of an active-site loop into a beta-hairpin and significant reorientation of a helix at the carboxy terminus. Interestingly, a new interface is formed between the ordered loop and the reoriented helix, both of which also form additional interactions with the coenzyme A moiety of the ligand. Site-directed mutation of the amino acid residues involved in these ligand-induced interactions significantly diminishes the enzyme activity. These results suggest a catalytically essential induced-fit that is likely initiated by the enzyme-ligand interactions at the active site.

Structural basis of the induced-fit mechanism of 1,4-dihydroxy-2-naphthoyl coenzyme a synthase from the crotonase fold superfamily.,Sun Y, Song H, Li J, Li Y, Jiang M, Zhou J, Guo Z PLoS One. 2013 Apr 26;8(4):e63095. doi: 10.1371/journal.pone.0063095. Print 2013. PMID:23658663<ref>PMID:23658663</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4i52" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synechocystis sp. PCC 6803 substr. Kazusa]]
[[Category: Guo ZH]]
[[Category: Jiang M]]
[[Category: Li J]]
[[Category: Li Y]]
[[Category: Song HG]]
[[Category: Sun YR]]
[[Category: Zhou JH]]