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| | <StructureSection load='1gqz' size='340' side='right'caption='[[1gqz]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='1gqz' size='340' side='right'caption='[[1gqz]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1gqz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haein Haein]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GQZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GQZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1gqz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae_Rd_KW20 Haemophilus influenzae Rd KW20]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GQZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GQZ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bwz|1bwz]]</div></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]] 1.75Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Diaminopimelate_epimerase Diaminopimelate epimerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.7 5.1.1.7] </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=1gqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gqz OCA], [https://pdbe.org/1gqz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gqz RCSB], [https://www.ebi.ac.uk/pdbsum/1gqz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gqz 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=1gqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gqz OCA], [https://pdbe.org/1gqz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gqz RCSB], [https://www.ebi.ac.uk/pdbsum/1gqz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gqz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/DAPF_HAEIN DAPF_HAEIN]] Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan. Only accepts DAP isomers with the L configuration.<ref>PMID:10194362</ref>
| + | [https://www.uniprot.org/uniprot/DAPF_HAEIN DAPF_HAEIN] Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan. Only accepts DAP isomers with the L configuration.<ref>PMID:10194362</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: Diaminopimelate epimerase]] | + | [[Category: Haemophilus influenzae Rd KW20]] |
| - | [[Category: Haein]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Huyton, T]] | + | [[Category: Huyton T]] |
| - | [[Category: Roper, D I]] | + | [[Category: Roper DI]] |
| - | [[Category: Turkenburg, J P]] | + | [[Category: Turkenburg JP]] |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Peptidoglycan biosynthesis]]
| + | |
| Structural highlights
Function
DAPF_HAEIN Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan. Only accepts DAP isomers with the L configuration.[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
Diaminopimelate (DAP) epimerase (DapF) is central to the biosynthesis of both lysine and cell-wall peptidoglycan in many bacteria species. The peptidoglycan layer provides great potential for the development of novel antimicrobials as it is a uniquely prokaryotic feature. Crystals of recombinant Haemophilus influenzae DapF that diffract to beyond 2 A resolution have been obtained which facilitated the solution of the structure by molecular replacement at a resolution approximately 1 A higher than that previously determined. An analysis of the structure (i) in comparison to other PLP-independent racemaces and (ii) in relation to the catalytic mechanism and stereospecificity of DapF is presented.
Refinement of Haemophilus influenzae diaminopimelic acid epimerase (DapF) at 1.75 A resolution suggests a mechanism for stereocontrol during catalysis.,Lloyd AJ, Huyton T, Turkenburg J, Roper DI Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):397-400. Epub 2004, Jan 23. PMID:14747737[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Koo CW, Blanchard JS. Chemical mechanism of Haemophilus influenzae diaminopimelate epimerase. Biochemistry. 1999 Apr 6;38(14):4416-22. PMID:10194362 doi:http://dx.doi.org/10.1021/bi982911f
- ↑ Lloyd AJ, Huyton T, Turkenburg J, Roper DI. Refinement of Haemophilus influenzae diaminopimelic acid epimerase (DapF) at 1.75 A resolution suggests a mechanism for stereocontrol during catalysis. Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):397-400. Epub 2004, Jan 23. PMID:14747737 doi:http://dx.doi.org/10.1107/S0907444903027999
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