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| | ==YHCH PROTEIN (HI0227) COPPER COMPLEX== | | ==YHCH PROTEIN (HI0227) COPPER COMPLEX== |
| - | <StructureSection load='1s4c' size='340' side='right' caption='[[1s4c]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='1s4c' size='340' side='right'caption='[[1s4c]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1s4c]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S4C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1S4C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1s4c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S4C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S4C FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jop|1jop]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HI0227 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 "Bacterium influenzae" Lehmann and Neumann 1896])</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=1s4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s4c OCA], [https://pdbe.org/1s4c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s4c RCSB], [https://www.ebi.ac.uk/pdbsum/1s4c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s4c ProSAT]</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=1s4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s4c OCA], [http://pdbe.org/1s4c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s4c RCSB], [http://www.ebi.ac.uk/pdbsum/1s4c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s4c ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/NANQ_HAEIN NANQ_HAEIN] Opens both the alpha- and beta-forms of N-acetylneuraminate (sialic acid; Neu5Ac) to provide aceneuramate, the preferred substrate for NanA (Probable). Has preferential activity on the beta-anomer rather than the alpha-anomer. Accelerates a reaction that is spontaneous at slightly alkaline pH, facilitates the reaction at acidic pH (By similarity).[UniProtKB:P45424]<ref>PMID:33895133</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacterium influenzae lehmann and neumann 1896]] | + | [[Category: Haemophilus influenzae]] |
| - | [[Category: Gilliland, G L]] | + | [[Category: Large Structures]] |
| - | [[Category: Obmolova, G]] | + | [[Category: Gilliland GL]] |
| - | [[Category: Teplyakov, A]] | + | [[Category: Obmolova G]] |
| - | [[Category: Toedt, J]] | + | [[Category: Teplyakov A]] |
| - | [[Category: Double-stranded beta-helix]]
| + | [[Category: Toedt J]] |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
NANQ_HAEIN Opens both the alpha- and beta-forms of N-acetylneuraminate (sialic acid; Neu5Ac) to provide aceneuramate, the preferred substrate for NanA (Probable). Has preferential activity on the beta-anomer rather than the alpha-anomer. Accelerates a reaction that is spontaneous at slightly alkaline pH, facilitates the reaction at acidic pH (By similarity).[UniProtKB:P45424][1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The yhcH gene is part of the nan operon in bacteria that encodes proteins involved in sialic acid catabolism. Determination of the crystal structure of YhcH from Haemophilus influenzae was undertaken as part of a structural genomics effort in order to assist with the functional assignment of the protein. The structure was determined at 2.2-A resolution by multiple-wavelength anomalous diffraction. The protein fold is a variation of the double-stranded beta-helix. Two antiparallel beta-sheets form a funnel opened at one side, where a putative active site contains a copper ion coordinated to the side chains of two histidine and two carboxylic acid residues. A comparison to other proteins with a similar fold and analysis of the genomic context suggested that YhcH may be a sugar isomerase involved in processing of exogenous sialic acid.
Crystal structure of the bacterial YhcH protein indicates a role in sialic acid catabolism.,Teplyakov A, Obmolova G, Toedt J, Galperin MY, Gilliland GL J Bacteriol. 2005 Aug;187(16):5520-7. PMID:16077096[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kentache T, Thabault L, Deumer G, Haufroid V, Frédérick R, Linster CL, Peracchi A, Veiga-da-Cunha M, Bommer GT, Van Schaftingen E. The metalloprotein YhcH is an anomerase providing N-acetylneuraminate aldolase with the open form of its substrate. J Biol Chem. 2021 Jan-Jun;296:100699. PMID:33895133 doi:10.1016/j.jbc.2021.100699
- ↑ Teplyakov A, Obmolova G, Toedt J, Galperin MY, Gilliland GL. Crystal structure of the bacterial YhcH protein indicates a role in sialic acid catabolism. J Bacteriol. 2005 Aug;187(16):5520-7. PMID:16077096 doi:187/16/5520
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