4bif: Difference between revisions
New page: '''Unreleased structure''' The entry 4bif is ON HOLD Authors: Hajnal, I., Lyskowski, A., Hanefeld, U., Gruber, K., Schwab, H., Steiner, K. Description: Biochemical and structural chara... |
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The | ==Biochemical and structural characterisation of a novel manganese- dependent hydroxynitrile lyase from bacteria== | ||
<StructureSection load='4bif' size='340' side='right'caption='[[4bif]], [[Resolution|resolution]] 2.46Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4bif]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Granulicella_tundricola_MP5ACTX9 Granulicella tundricola MP5ACTX9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BIF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BIF 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]] 2.46Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=4bif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bif OCA], [https://pdbe.org/4bif PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bif RCSB], [https://www.ebi.ac.uk/pdbsum/4bif PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bif ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/E8WYN5_GRATM E8WYN5_GRATM] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Hydroxynitrile lyases (HNLs), which catalyse the decomposition of cyanohydrins, are found mainly in plants. In vitro they are able to catalyse the synthesis of enantiopure cyanohydrins, which are versatile building blocks in chemical industry. Recently, HNLs have also been discovered in bacteria. Here, we report on the detailed biochemical and structural characterisation of a hydroxynitrile lyase from Granulicella tundricola (GtHNL), which was successfully heterologously expressed in E. coli. The crystal structure was solved at a crystallographic resolution of 2.5 A and exhibits a cupin fold. As GtHNL does not show any sequence or structural similarity to any other HNL nor contains conserved motifs typical for HNLs, cupins represent a new class of HNLs. GtHNL is metal-dependent as confirmed by ICP-OES and in the structure manganese is bound to three histidine and one glutamine residue. GtHNL displayed a specific activity of 1.74 U mg-1 at pH 6 with (R)-mandelonitrile, and synthesised (R)-mandelonitrile with 90% ee, at 80% conversion of 0.5 M benzaldehyde in a biphasic reaction system with MTBE. This article is protected by copyright. All rights reserved. | |||
Biochemical and structural characterisation of a novel bacterial manganese-dependent hydroxynitrile lyase.,Hajnal I, Lyskowski A, Hanefeld U, Gruber K, Schwab H, Steiner K FEBS J. 2013 Aug 25. doi: 10.1111/febs.12501. PMID:23981508<ref>PMID:23981508</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4bif" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Granulicella tundricola MP5ACTX9]] | |||
[[Category: Large Structures]] | |||
[[Category: Gruber K]] | |||
[[Category: Hajnal I]] | |||
[[Category: Hanefeld U]] | |||
[[Category: Lyskowski A]] | |||
[[Category: Schwab H]] | |||
[[Category: Steiner K]] | |||
Latest revision as of 14:52, 20 December 2023
Biochemical and structural characterisation of a novel manganese- dependent hydroxynitrile lyase from bacteriaBiochemical and structural characterisation of a novel manganese- dependent hydroxynitrile lyase from bacteria
Structural highlights
FunctionPublication Abstract from PubMedHydroxynitrile lyases (HNLs), which catalyse the decomposition of cyanohydrins, are found mainly in plants. In vitro they are able to catalyse the synthesis of enantiopure cyanohydrins, which are versatile building blocks in chemical industry. Recently, HNLs have also been discovered in bacteria. Here, we report on the detailed biochemical and structural characterisation of a hydroxynitrile lyase from Granulicella tundricola (GtHNL), which was successfully heterologously expressed in E. coli. The crystal structure was solved at a crystallographic resolution of 2.5 A and exhibits a cupin fold. As GtHNL does not show any sequence or structural similarity to any other HNL nor contains conserved motifs typical for HNLs, cupins represent a new class of HNLs. GtHNL is metal-dependent as confirmed by ICP-OES and in the structure manganese is bound to three histidine and one glutamine residue. GtHNL displayed a specific activity of 1.74 U mg-1 at pH 6 with (R)-mandelonitrile, and synthesised (R)-mandelonitrile with 90% ee, at 80% conversion of 0.5 M benzaldehyde in a biphasic reaction system with MTBE. This article is protected by copyright. All rights reserved. Biochemical and structural characterisation of a novel bacterial manganese-dependent hydroxynitrile lyase.,Hajnal I, Lyskowski A, Hanefeld U, Gruber K, Schwab H, Steiner K FEBS J. 2013 Aug 25. doi: 10.1111/febs.12501. PMID:23981508[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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