6eb0: Difference between revisions
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<StructureSection load='6eb0' size='340' side='right'caption='[[6eb0]], [[Resolution|resolution]] 2.37Å' scene=''> | <StructureSection load='6eb0' size='340' side='right'caption='[[6eb0]], [[Resolution|resolution]] 2.37Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6eb0]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EB0 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6eb0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EB0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EB0 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.37Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</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=6eb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eb0 OCA], [https://pdbe.org/6eb0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6eb0 RCSB], [https://www.ebi.ac.uk/pdbsum/6eb0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6eb0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A140NG21_ECOBD A0A140NG21_ECOBD] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6eb0" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6eb0" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kandavelu | [[Category: Kandavelu P]] | ||
[[Category: Rose | [[Category: Rose J]] | ||
[[Category: Wang | [[Category: Wang BC]] | ||
[[Category: Yan | [[Category: Yan Y]] | ||
[[Category: Zhang | [[Category: Zhang H]] | ||
[[Category: Zhou | [[Category: Zhou D]] | ||
Latest revision as of 09:22, 11 October 2023
STRUCTURE OF 4-HYDROXYPHENYLACETATE 3-MONOOXYGENASE (HPAB), OXYGENASE COMPONENT FROM ESCHERICHIA COLISTRUCTURE OF 4-HYDROXYPHENYLACETATE 3-MONOOXYGENASE (HPAB), OXYGENASE COMPONENT FROM ESCHERICHIA COLI
Structural highlights
FunctionPublication Abstract from PubMed4-Hydroxyphenylacetate 3-hydroxylase (EcHpaB) from Escherichia coli is capable of efficient ortho-hydroxylation of a wide range of phenolic compounds and demonstrates great potential for broad chemoenzymatic applications. To understand the structural and mechanistic basis of its catalytic versatility, we elucidated the crystal structure of EcHpaB by X-ray crystallography, which revealed a unique loop structure covering the active site. We further performed mutagenesis studies of this loop to probe its role in substrate specificity and catalytic activity. Our results not only showed the loop has great plasticity and strong tolerance towards extensive mutagenesis, but also suggested a flexible loop that enables the entrance and stable binding of substrates into the active site is the key factor to the enzyme catalytic versatility. These findings lay the groundwork for editing the loop sequence and structure for generation of EcHpaB mutants with improved performance for broader laboratory and industrial use. Structural Insights into Catalytic Versatility of the Flavin-dependent Hydroxylase (HpaB) from Escherichia coli.,Shen X, Zhou D, Lin Y, Wang J, Gao S, Kandavelu P, Zhang H, Zhang R, Wang BC, Rose J, Yuan Q, Yan Y Sci Rep. 2019 May 8;9(1):7087. doi: 10.1038/s41598-019-43577-w. PMID:31068633[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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