5xw2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "5xw2" [edit=sysop:move=sysop])
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 5xw2 is ON HOLD
+
==Crystal structure of the Hydroxylase HmtN in C 1 2 1 crystal form==
 +
<StructureSection load='5xw2' size='340' side='right' caption='[[5xw2]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[5xw2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XW2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XW2 FirstGlance]. <br>
 +
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 +
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4e2p|4e2p]]</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=5xw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xw2 OCA], [http://pdbe.org/5xw2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xw2 RCSB], [http://www.ebi.ac.uk/pdbsum/5xw2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xw2 ProSAT]</span></td></tr>
 +
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Himastatin is a novel antibiotic with antitumor and antibacterial activity. In the himastatin biosynthesis pathway, HmtN is responsible for the hydroxylation of the piperazic acid (Pip) motif. Herein, we present the crystal structures of HmtN (1.3 A), which is the first structure for a cytochrome P450 involved in the hydroxylation of cyclohexadepsipeptide during himastatin biosynthesis. Structure analysis indicated that almost all the surface of HmtN has negative electrostatic potential, only small patches of positive electrostatic potential can be found. It is worth noting that almost the entire active site of HmtT is negatively charged, while HmtN active site is composed of positive and negative charge. This may be relevant to their specific substrate recognition and different catalytic function. In addition, three channels were observed in HmtN crystal structure; channel 3 may be essential for substrate ingress and egress from the active site to the surface, while channel 1 and channel 2 may be the solvent and water pathway, respectively.
-
Authors: Zhang, H.D., Zhang, H.J.
+
Molecular characterization of the hydroxylase HmtN at 1.3 A resolution.,Zhang H, Chen J, Zhang H Biochem Biophys Res Commun. 2017 Jul 4. pii: S0006-291X(17)31341-4. doi:, 10.1016/j.bbrc.2017.07.010. PMID:28687492<ref>PMID:28687492</ref>
-
Description: Crystal structure of the Hydroxylase HmtN in C 1 2 1 crystal form
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
-
[[Category: Zhang, H.J]]
+
<div class="pdbe-citations 5xw2" style="background-color:#fffaf0;"></div>
-
[[Category: Zhang, H.D]]
+
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Zhang, H D]]
 +
[[Category: Zhang, H J]]
 +
[[Category: Biosynthetic protein]]
 +
[[Category: Cytochrome p450]]
 +
[[Category: Himastatin]]
 +
[[Category: Hydroxylase]]

Revision as of 05:29, 25 April 2018

Crystal structure of the Hydroxylase HmtN in C 1 2 1 crystal form

5xw2, resolution 1.30Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5xw2"
Personal tools