View source for 4ggv


==Crystal Structure of HmtT Involved in Himastatin Biosynthesis==
<StructureSection load='4ggv' size='340' side='right'caption='[[4ggv]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ggv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_himastatinicus_ATCC_53653 Streptomyces himastatinicus ATCC 53653]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GGV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GGV 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]] 2.331&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=4ggv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ggv OCA], [https://pdbe.org/4ggv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ggv RCSB], [https://www.ebi.ac.uk/pdbsum/4ggv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ggv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D9WMR2_9ACTN D9WMR2_9ACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Himastatin is a novel antibiotic featuring a bicyclohexadepsipeptide structure. On the himastatin biosynthesis pathway, three cytochrome P450s (HmtT, HmtN, HmtS) are responsible for the post-tailoring of the cyclohexadepsipeptide backbone. Here we report the crystal structures of HmtT and HmtN. The overall structures of these two proteins are homologous to other cytochrome P450s. However, the exceptionally long F-G loop in HmtT has a highly unusual conformation and extends deep into the active site. As a result, the F/G helices of HmtT are both kinked. In contrast, the F/G helices of HmtN are straight. Also, the F/G helices in HmtT and HmtN take distinctive orientations, which may be a contributing factor for the substrate specificity of these two enzymes.

Structural analysis of HmtT and HmtN involved in the tailoring steps of himastatin biosynthesis.,Zhang H, Chen J, Wang H, Xie Y, Ju J, Yan Y, Zhang H FEBS Lett. 2013 Jun 5;587(11):1675-80. doi: 10.1016/j.febslet.2013.04.013. Epub, 2013 Apr 20. PMID:23611984<ref>PMID:23611984</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ggv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces himastatinicus ATCC 53653]]
[[Category: Chen J]]
[[Category: Wang H]]
[[Category: Zhang H]]