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| | <StructureSection load='6t3t' size='340' side='right'caption='[[6t3t]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='6t3t' size='340' side='right'caption='[[6t3t]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6t3t]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Methylacidiphilum_fumariolicum_solv Methylacidiphilum fumariolicum solv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T3T OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6T3T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6t3t]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylacidiphilum_fumariolicum_SolV Methylacidiphilum fumariolicum SolV]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T3T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T3T FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.1Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxy-tetrahydrodipicolinate_synthase 4-hydroxy-tetrahydrodipicolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.3.7 4.3.3.7] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6t3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t3t OCA], [http://pdbe.org/6t3t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6t3t RCSB], [http://www.ebi.ac.uk/pdbsum/6t3t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6t3t ProSAT]</span></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=6t3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t3t OCA], [https://pdbe.org/6t3t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t3t RCSB], [https://www.ebi.ac.uk/pdbsum/6t3t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t3t ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/I0JZ23_METFB I0JZ23_METFB]] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[HAMAP-Rule:MF_00418][SAAS:SAAS00570606] | + | [https://www.uniprot.org/uniprot/I0JZ23_METFB I0JZ23_METFB] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[HAMAP-Rule:MF_00418][SAAS:SAAS00570606] |
| | <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: 4-hydroxy-tetrahydrodipicolinate synthase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Methylacidiphilum fumariolicum solv]] | + | [[Category: Methylacidiphilum fumariolicum SolV]] |
| - | [[Category: Barends, T]] | + | [[Category: Barends T]] |
| - | [[Category: Berben, T]] | + | [[Category: Berben T]] |
| - | [[Category: Camp, H Op den]]
| + | [[Category: Dietl A]] |
| - | [[Category: Dietl, A]] | + | [[Category: Mueller M]] |
| - | [[Category: Mueller, M]] | + | [[Category: Op den Camp H]] |
| - | [[Category: Schmitz, R]] | + | [[Category: Schmitz R]] |
| - | [[Category: Lyase]] | + | |
| - | [[Category: Lysine biosynthesis]]
| + | |
| - | [[Category: Methanotrophy]]
| + | |
| - | [[Category: Thermoacidophile]]
| + | |
| Structural highlights
Function
I0JZ23_METFB Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[HAMAP-Rule:MF_00418][SAAS:SAAS00570606]
Publication Abstract from PubMed
The enzyme 4-hydroxy-tetrahydrodipicolinate synthase (DapA) is involved in the production of lysine and precursor molecules for peptidoglycan synthesis. In a multistep reaction, DapA converts pyruvate and L-aspartate-4-semialdehyde to 4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid. In many organisms, lysine binds allosterically to DapA, causing negative feedback, thus making the enzyme an important regulatory component of the pathway. Here, the 2.1 A resolution crystal structure of DapA from the thermoacidophilic methanotroph Methylacidiphilum fumariolicum SolV is reported. The enzyme crystallized as a contaminant of a protein preparation from native biomass. Genome analysis reveals that M. fumariolicum SolV utilizes the recently discovered aminotransferase pathway for lysine biosynthesis. Phylogenetic analyses of the genes involved in this pathway shed new light on the distribution of this pathway across the three domains of life.
Structure of the 4-hydroxy-tetrahydrodipicolinate synthase from the thermoacidophilic methanotroph Methylacidiphilum fumariolicum SolV and the phylogeny of the aminotransferase pathway.,Schmitz RA, Dietl A, Muller M, Berben T, Op den Camp HJM, Barends TRM Acta Crystallogr F Struct Biol Commun. 2020 May 1;76(Pt 5):199-208. doi:, 10.1107/S2053230X20005294. Epub 2020 Apr 28. PMID:32356521[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schmitz RA, Dietl A, Muller M, Berben T, Op den Camp HJM, Barends TRM. Structure of the 4-hydroxy-tetrahydrodipicolinate synthase from the thermoacidophilic methanotroph Methylacidiphilum fumariolicum SolV and the phylogeny of the aminotransferase pathway. Acta Crystallogr F Struct Biol Commun. 2020 May 1;76(Pt 5):199-208. doi:, 10.1107/S2053230X20005294. Epub 2020 Apr 28. PMID:32356521 doi:http://dx.doi.org/10.1107/S2053230X20005294
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