View source for 4e1o


==Human histidine decarboxylase complex with Histidine methyl ester (HME)==
<StructureSection load='4e1o' size='340' side='right'caption='[[4e1o]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4e1o]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E1O 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PVH:HISTIDINE-METHYL-ESTER'>PVH</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=4e1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1o OCA], [https://pdbe.org/4e1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e1o RCSB], [https://www.ebi.ac.uk/pdbsum/4e1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e1o ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DCHS_HUMAN DCHS_HUMAN] Catalyzes the biosynthesis of histamine from histidine.<ref>PMID:22767596</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Histamine is an important chemical mediator for a wide variety of physiological reactions. L-histidine decarboxylase (HDC) is the primary enzyme responsible for histamine synthesis and produces histamine from histidine in a one-step reaction. In this study, we determined the crystal structure of human HDC (hHDC) complexed with the inhibitor histidine methyl ester (HME). This structure shows the detailed features of the pyridoxal-5'-phosphate (PLP)-inhibitor adduct (external aldimine) at the active site of HDC. Moreover, a comparison of the structures of hHDC and aromatic L-amino acid (L-dopa) decarboxylase showed that Ser354 (S345) was a key residue for substrate specificity. The S354G mutation at the active site enlarged the size of the hHDC substrate-binding pocket and resulted in a decreased affinity for histidine, but an acquired ability to bind and act on L-dopa as a substrate. These data provide insight into the molecular basis of substrate recognition among the group II PLP-dependent decarboxylases.

Structural study reveals Ser345 determines substrate specificity on human histidine decarboxylase.,Komori H, Nitta Y, Ueno H, Higuchi Y J Biol Chem. 2012 Jul 5. PMID:22767596<ref>PMID:22767596</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4e1o" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Higuchi Y]]
[[Category: Komori H]]
[[Category: Nitta Y]]
[[Category: Ueno H]]