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==CRYSTAL STRUCTURE OF THE D248N mutant of 2-PYRONE-4,6-DICARBOXYLIC ACID HYDROLASE FROM SPHINGOMONAS PAUCIMOBILIS complexed with substrate at pH 4.6==
==CRYSTAL STRUCTURE OF THE D248N mutant of 2-PYRONE-4,6-DICARBOXYLIC ACID HYDROLASE FROM SPHINGOMONAS PAUCIMOBILIS complexed with substrate at pH 4.6==
<StructureSection load='4dia' size='340' side='right' caption='[[4dia]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='4dia' size='340' side='right'caption='[[4dia]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4dia]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_devorans"_zimmermann_1890 "bacillus devorans" zimmermann 1890]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4d9d 4d9d]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DIA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DIA FirstGlance]. <br>
<table><tr><td colspan='2'>[[4dia]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingomonas_paucimobilis Sphingomonas paucimobilis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4d9d 4d9d]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DIA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DIA FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2qah|2qah]], [[4d8l|4d8l]], [[4di8|4di8]], [[4di9|4di9]]</td></tr>
</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=4dia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dia OCA], [https://pdbe.org/4dia PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dia RCSB], [https://www.ebi.ac.uk/pdbsum/4dia PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dia ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ligI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=13689 "Bacillus devorans" Zimmermann 1890])</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=4dia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dia OCA], [http://pdbe.org/4dia PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dia RCSB], [http://www.ebi.ac.uk/pdbsum/4dia PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dia ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PDCH_SPHPI PDCH_SPHPI]] Plays an important role in the metabolism of lignin-derived aromatic compounds. Involved in the meta fission degradative pathway of protocatechuate. Catalyzes the reversible hydrolysis of 2-pyrone-4,6-dicarboxylate (PDC) to a mixture of 4-carboxy-2-hydroxymuconate (CHM) and 4-oxalomesaconate (OMA). The product of the enzymatic reaction exists in two forms depending on the pH. At pH 10, the keto form (OMA) is predominant, and at pH 6, the enol form (CHM) is predominant (PubMed:22475079).<ref>PMID:22475079</ref> <ref>PMID:7142106</ref> <ref>PMID:9864312</ref>
[[https://www.uniprot.org/uniprot/LIGI_SPHSK LIGI_SPHSK]] Contributes to the degradation of lignin at the level of the protocatechuate 4,5-cleavage pathway (PubMed:9864312). Catalyzes the hydrolysis of 2-pyrone-4,6-dicarboxylate (PDC) to (4E)-oxalomesaconate (OMA) (PubMed:29658701, PubMed:22475079). The keto form of OMA can tautomerize into the enol form, 4-carboxy-2-hydroxymuconate (CHM), under certain pH conditions (PubMed:22475079). Also catalyzes the reverse reaction (PubMed:22475079, PubMed:9864312). Is essential for the growth of Sphingobium sp. SYK-6 on vanillate but is not responsible for the growth of this strain on syringate (PubMed:9864312).<ref>PMID:22475079</ref> <ref>PMID:29658701</ref> <ref>PMID:9864312</ref>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus devorans zimmermann 1890]]
[[Category: Large Structures]]
[[Category: Almo, S C]]
[[Category: Sphingomonas paucimobilis]]
[[Category: Hobbs, M E]]
[[Category: Almo SC]]
[[Category: Malashkevich, V N]]
[[Category: Hobbs ME]]
[[Category: Raushel, F M]]
[[Category: Malashkevich VN]]
[[Category: Toro, R]]
[[Category: Raushel FM]]
[[Category: Hydrolase]]
[[Category: Toro R]]
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