|
|
| (One intermediate revision not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Human histidine decarboxylase complex with Histidine methyl ester (HME)== | | ==Human histidine decarboxylase complex with Histidine methyl ester (HME)== |
| - | <StructureSection load='4e1o' size='340' side='right' caption='[[4e1o]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='4e1o' size='340' side='right'caption='[[4e1o]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4e1o]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E1O FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PVH:HISTIDINE-METHYL-ESTER'>PVH</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HDC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histidine_decarboxylase Histidine decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.22 4.1.1.22] </span></td></tr> | + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4e1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e1o OCA], [http://pdbe.org/4e1o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e1o RCSB], [http://www.ebi.ac.uk/pdbsum/4e1o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4e1o ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DCHS_HUMAN DCHS_HUMAN]] Catalyzes the biosynthesis of histamine from histidine.<ref>PMID:22767596</ref> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 25: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Histidine decarboxylase]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]] | + | [[Category: Large Structures]] |
| - | [[Category: Higuchi, Y]] | + | [[Category: Higuchi Y]] |
| - | [[Category: Komori, H]] | + | [[Category: Komori H]] |
| - | [[Category: Nitta, Y]] | + | [[Category: Nitta Y]] |
| - | [[Category: Ueno, H]] | + | [[Category: Ueno H]] |
| - | [[Category: Lyase]]
| + | |
| Structural highlights
Function
DCHS_HUMAN Catalyzes the biosynthesis of histamine from histidine.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Komori H, Nitta Y, Ueno H, Higuchi Y. Structural study reveals Ser345 determines substrate specificity on human histidine decarboxylase. J Biol Chem. 2012 Jul 5. PMID:22767596 doi:10.1074/jbc.M112.381897
- ↑ Komori H, Nitta Y, Ueno H, Higuchi Y. Structural study reveals Ser345 determines substrate specificity on human histidine decarboxylase. J Biol Chem. 2012 Jul 5. PMID:22767596 doi:10.1074/jbc.M112.381897
|
