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| | <StructureSection load='5ktl' size='340' side='right'caption='[[5ktl]], [[Resolution|resolution]] 1.92Å' scene=''> | | <StructureSection load='5ktl' size='340' side='right'caption='[[5ktl]], [[Resolution|resolution]] 1.92Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ktl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_atcc29413 Anabaena atcc29413]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KTL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5KTL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ktl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichormus_variabilis_ATCC_29413 Trichormus variabilis ATCC 29413]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KTL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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]] 1.92Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KPI:(2S)-2-AMINO-6-[(1-HYDROXY-1-OXO-PROPAN-2-YLIDENE)AMINO]HEXANOIC+ACID'>KPI</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KPI:(2S)-2-AMINO-6-[(1-HYDROXY-1-OXO-PROPAN-2-YLIDENE)AMINO]HEXANOIC+ACID'>KPI</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kt0|5kt0]]</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=5ktl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ktl OCA], [https://pdbe.org/5ktl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ktl RCSB], [https://www.ebi.ac.uk/pdbsum/5ktl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ktl ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dapA, Ava_3607 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=240292 Anabaena ATCC29413])</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ktl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ktl OCA], [http://pdbe.org/5ktl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ktl RCSB], [http://www.ebi.ac.uk/pdbsum/5ktl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ktl ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q3M723_ANAVT Q3M723_ANAVT]] 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/Q3M723_TRIV2 Q3M723_TRIV2] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[ARBA:ARBA00003294][HAMAP-Rule:MF_00418] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5ktl" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5ktl" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Dihydrodipicolinate synthase|Dihydrodipicolinate synthase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 4-hydroxy-tetrahydrodipicolinate synthase]] | |
| - | [[Category: Anabaena atcc29413]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Christensen, J B]] | + | [[Category: Trichormus variabilis ATCC 29413]] |
| - | [[Category: Panjikar, S]] | + | [[Category: Christensen JB]] |
| - | [[Category: Perugini, M]] | + | [[Category: Panjikar S]] |
| - | [[Category: Cyanobacteria]] | + | [[Category: Perugini M]] |
| - | [[Category: Dhdp]]
| + | |
| - | [[Category: Diaminopimelate biosynthesis pathway]]
| + | |
| - | [[Category: Enzyme]]
| + | |
| - | [[Category: Lyase]]
| + | |
| Structural highlights
Function
Q3M723_TRIV2 Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[ARBA:ARBA00003294][HAMAP-Rule:MF_00418]
Publication Abstract from PubMed
Lysine biosynthesis in bacteria and plants commences with a condensation reaction catalysed by dihydrodipicolinate synthase (DHDPS) followed by a reduction reaction catalysed by dihydrodipicolinate reductase (DHDPR). Interestingly, both DHDPS and DHDPR exist as different oligomeric forms in bacteria and plants. DHDPS is primarily a homotetramer in all species, but the architecture of the tetramer differs across kingdoms. DHDPR also exists as a tetramer in bacteria, but has recently been reported to be dimeric in plants. This study aimed to characterise for the first time the structure and function of DHDPS and DHDPR from cyanobacteria, which is an evolutionary important phylum that evolved at the divergence point between bacteria and plants. We cloned, expressed and purified DHDPS and DHDPR from the cyanobacterium Anabaena variabilis. The recombinant enzymes were shown to be folded by circular dichroism spectroscopy, enzymatically active employing the quantitative DHDPS-DHDPR coupled assay, and form tetramers in solution using analytical ultracentrifugation. Crystal structures of DHDPS and DHDPR from A. variabilis were determined at 1.92 A and 2.83 A, respectively, and show that both enzymes adopt the canonical bacterial tetrameric architecture. These studies indicate that the quaternary structure of bacterial and plant DHDPS and DHDPR diverged after cyanobacteria evolved.
Structure and Function of Cyanobacterial DHDPS and DHDPR.,Christensen JB, Soares da Costa TP, Faou P, Pearce FG, Panjikar S, Perugini MA Sci Rep. 2016 Nov 15;6:37111. doi: 10.1038/srep37111. PMID:27845445[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Christensen JB, Soares da Costa TP, Faou P, Pearce FG, Panjikar S, Perugini MA. Structure and Function of Cyanobacterial DHDPS and DHDPR. Sci Rep. 2016 Nov 15;6:37111. doi: 10.1038/srep37111. PMID:27845445 doi:http://dx.doi.org/10.1038/srep37111
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