5xw2: Difference between revisions
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<StructureSection load='5xw2' size='340' side='right'caption='[[5xw2]], [[Resolution|resolution]] 1.30Å' scene=''> | <StructureSection load='5xw2' size='340' side='right'caption='[[5xw2]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
== Structural highlights == | == 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 [ | <table><tr><td colspan='2'>[[5xw2]] 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=5XW2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XW2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.298Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5xw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xw2 OCA], [https://pdbe.org/5xw2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xw2 RCSB], [https://www.ebi.ac.uk/pdbsum/5xw2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xw2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/D9WMQ6_9ACTN D9WMQ6_9ACTN] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Streptomyces himastatinicus ATCC 53653]] | ||
[[Category: Zhang | [[Category: Zhang HD]] | ||
[[Category: | [[Category: Zhang HJ]] | ||
Latest revision as of 11:15, 22 November 2023
Crystal structure of the Hydroxylase HmtN in C 1 2 1 crystal formCrystal structure of the Hydroxylase HmtN in C 1 2 1 crystal form
Structural highlights
FunctionPublication Abstract from PubMedHimastatin 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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