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| | <StructureSection load='5fag' size='340' side='right'caption='[[5fag]], [[Resolution|resolution]] 1.51Å' scene=''> | | <StructureSection load='5fag' size='340' side='right'caption='[[5fag]], [[Resolution|resolution]] 1.51Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5fag]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Strco Strco]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FAG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FAG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5fag]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor_A3(2) Streptomyces coelicolor A3(2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FAG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PPI:PROPANOIC+ACID'>PPI</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]] 1.51Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PPI:PROPANOIC+ACID'>PPI</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">alr, SCO4745, SC6G4.23 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=100226 STRCO])</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=5fag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fag OCA], [https://pdbe.org/5fag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fag RCSB], [https://www.ebi.ac.uk/pdbsum/5fag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fag ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alanine_racemase Alanine racemase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.1 5.1.1.1] </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=5fag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fag OCA], [http://pdbe.org/5fag PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fag RCSB], [http://www.ebi.ac.uk/pdbsum/5fag PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fag ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ALR_STRCO ALR_STRCO]] Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. | + | [https://www.uniprot.org/uniprot/ALR_STRCO ALR_STRCO] Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids. |
| | <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: Alanine racemase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Strco]]
| + | [[Category: Pannu NS]] |
| - | [[Category: Pannu, N S]] | + | [[Category: Tassoni R]] |
| - | [[Category: Tassoni, R]] | + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Plp]]
| + | |
| - | [[Category: Propionate]]
| + | |
| Structural highlights
5fag is a 4 chain structure with sequence from Streptomyces coelicolor A3(2). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.51Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
ALR_STRCO Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
Publication Abstract from PubMed
The conversion of l-alanine (L-Ala) into d-alanine (D-Ala) in bacteria is performed by pyridoxal phosphate-dependent enzymes called alanine racemases. D-Ala is an essential component of the bacterial peptidoglycan and hence required for survival. The Gram-positive bacterium Streptomyces coelicolor has at least one alanine racemase encoded by alr. Here, we describe an alr deletion mutant of S. coelicolor which depends on D-Ala for growth and shows increased sensitivity to the antibiotic d-cycloserine (DCS). The crystal structure of the alanine racemase (Alr) was solved with and without the inhibitors DCS or propionate, at 1.64 A and 1.51 A resolution, respectively. The crystal structures revealed that Alr is a homodimer with residues from both monomers contributing to the active site. The dimeric state of the enzyme in solution was confirmed by gel filtration chromatography, with and without L-Ala or d-cycloserine. The activity of the enzyme was 66 +/- 3 U mg-1 for the racemization of L- to D-Ala, and 104 +/- 7 U mg-1 for the opposite direction. Comparison of Alr from S. coelicolor with orthologous enzymes from other bacteria, including the closely related d-cycloserine-resistant Alr from S. lavendulae, strongly suggests that structural features such as the hinge angle or the surface area between the monomers do not contribute to d-cycloserine resistance, and the molecular basis for resistance therefore remains elusive.
Structural and functional characterization of the alanine racemase from Streptomyces coelicolor A3(2).,Tassoni R, van der Aart LT, Ubbink M, van Wezel GP, Pannu NS Biochem Biophys Res Commun. 2017 Jan 29;483(1):122-128. doi:, 10.1016/j.bbrc.2016.12.183. Epub 2016 Dec 29. PMID:28042035[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tassoni R, van der Aart LT, Ubbink M, van Wezel GP, Pannu NS. Structural and functional characterization of the alanine racemase from Streptomyces coelicolor A3(2). Biochem Biophys Res Commun. 2017 Jan 29;483(1):122-128. doi:, 10.1016/j.bbrc.2016.12.183. Epub 2016 Dec 29. PMID:28042035 doi:http://dx.doi.org/10.1016/j.bbrc.2016.12.183
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