View source for 7eru


==Crystal structure of L-histidine decarboxylase (C57S mutant) from Photobacterium phosphoreum==
<StructureSection load='7eru' size='340' side='right'caption='[[7eru]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7eru]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Photobacterium_phosphoreum Photobacterium phosphoreum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ERU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ERU 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]] 2.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</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=7eru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eru OCA], [https://pdbe.org/7eru PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eru RCSB], [https://www.ebi.ac.uk/pdbsum/7eru PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eru ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q1JU62_PHOPO Q1JU62_PHOPO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Enzymatic amino acid assays are important in physiological research and clinical diagnostics because abnormal amino acid concentrations in biofluids are associated with various diseases. L-histidine decarboxylase from Photobacterium phosphoreum (PpHDC) is a pyridoxal 5'-phosphate-dependent enzyme and a candidate for use in an L-histidine quantitation assay. Previous cysteine substitution experiments demonstrated that the PpHDC C57S mutant displayed improved long-term storage stability and thermostability when compared with those of the wild-type enzyme. In this study, combinational mutation experiments of single cysteine substitution mutants of PpHDC were performed, revealing that the PpHDC C57S/C101V/C282V mutant possessed the highest thermostability. The stabilizing mechanism of these mutations was elucidated by solving the structures of PpHDC C57S and C57S/C101V/C282V mutants by X-ray crystallography. In the crystal structures, two symmetry-related PpHDC molecules form a domain-swapped homodimer. The side chain of S57 is solvent exposed in the structure, indicating that the C57S mutation eliminates chemical oxidation or disulfide bond formation with a free thiol group, thereby providing greater stability. Residues 101 and 282 form hydrophobic interactions with neighboring hydrophobic residues. Mutations C101V and C282V enhanced thermostability of PpHDC by filling a cavity present in the hydrophobic core (C101V) and increasing hydrophobic interactions.

Structural insights into the enhanced thermostability of cysteine substitution mutants of L-histidine decarboxylase from Photobacterium phosphoreum.,Oda Y, Nakata K, Miyano H, Mizukoshi T, Yamaguchi H, Kashiwagi T J Biochem. 2022 Jan 7;171(1):31-40. doi: 10.1093/jb/mvab103. PMID:34622278<ref>PMID:34622278</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7eru" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Photobacterium phosphoreum]]
[[Category: Kashiwagi T]]
[[Category: Miyano H]]
[[Category: Mizukoshi T]]
[[Category: Nakata K]]
[[Category: Oda Y]]
[[Category: Yamaguchi H]]