|
|
| Line 3: |
Line 3: |
| | <StructureSection load='4a3q' size='340' side='right'caption='[[4a3q]], [[Resolution|resolution]] 2.15Å' scene=''> | | <StructureSection load='4a3q' size='340' side='right'caption='[[4a3q]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4a3q]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A3Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4A3Q FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4a3q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A3Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A3Q FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alanine_racemase Alanine racemase], with EC number [https://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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4a3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a3q OCA], [http://pdbe.org/4a3q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a3q RCSB], [http://www.ebi.ac.uk/pdbsum/4a3q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a3q 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=4a3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a3q OCA], [https://pdbe.org/4a3q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a3q RCSB], [https://www.ebi.ac.uk/pdbsum/4a3q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a3q ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ALR1_STAAM ALR1_STAAM]] Catalyzes the interconversion of L-alanine and D-alanine.<ref>PMID:22194336</ref> | + | [[https://www.uniprot.org/uniprot/ALR1_STAAM ALR1_STAAM]] Catalyzes the interconversion of L-alanine and D-alanine.<ref>PMID:22194336</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 27: |
Line 27: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Alanine racemase]] | | [[Category: Alanine racemase]] |
| | + | [[Category: Large Structures]] |
| | [[Category: Krause, K L]] | | [[Category: Krause, K L]] |
| | [[Category: Luckner, S R]] | | [[Category: Luckner, S R]] |
| Structural highlights
Function
[ALR1_STAAM] Catalyzes the interconversion of L-alanine and D-alanine.[1]
Publication Abstract from PubMed
Staphylococcus aureus is an opportunistic Gram-positive bacterium which causes a wide variety of diseases ranging from minor skin infections to potentially fatal conditions such as pneumonia, meningitis and septicaemia. The pathogen is a leading cause of nosocomial acquired infections, a problem that is exacerbated by the existence of methicillin- and glycopeptide antibiotic-resistant strains which can be challenging to treat. Alanine racemase (Alr) is a pyridoxal-5'-phosphate-dependent enzyme which catalyzes reversible racemization between enantiomers of alanine. As D-alanine is an essential component of the bacterial cell-wall peptidoglycan, inhibition of Alr is lethal to prokaryotes. Additionally, while ubiquitous amongst bacteria, this enzyme is absent in humans and most eukaryotes, making it an excellent antibiotic drug target. The crystal structure of S. aureus alanine racemase (Alr(Sas)), the sequence of which corresponds to that from the highly antibiotic-resistant Mu50 strain, has been solved to 2.15 A resolution. Comparison of the Alr(Sas) structure with those of various alanine racemases demonstrates a conserved overall fold, with the enzyme sharing most similarity to those from other Gram-positive bacteria. Structural examination indicates that the active-site binding pocket, dimer interface and active-site entryway of the enzyme are potential targets for structure-aided inhibitor design. Kinetic constants were calculated in this study and are reported here. The potential for a disulfide bond in this structure is noted. This structural and biochemical information provides a template for future structure-based drug-development efforts targeting Alr(Sas).
Structural features and kinetic characterization of alanine racemase from Staphylococcus aureus (Mu50).,Scaletti ER, Luckner SR, Krause KL Acta Crystallogr D Biol Crystallogr. 2012 Jan;68(Pt 1):82-92. Epub 2011 Dec 9. PMID:22194336[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Scaletti ER, Luckner SR, Krause KL. Structural features and kinetic characterization of alanine racemase from Staphylococcus aureus (Mu50). Acta Crystallogr D Biol Crystallogr. 2012 Jan;68(Pt 1):82-92. Epub 2011 Dec 9. PMID:22194336 doi:10.1107/S0907444911050682
- ↑ Scaletti ER, Luckner SR, Krause KL. Structural features and kinetic characterization of alanine racemase from Staphylococcus aureus (Mu50). Acta Crystallogr D Biol Crystallogr. 2012 Jan;68(Pt 1):82-92. Epub 2011 Dec 9. PMID:22194336 doi:10.1107/S0907444911050682
|
