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| | <StructureSection load='1xfc' size='340' side='right'caption='[[1xfc]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='1xfc' size='340' side='right'caption='[[1xfc]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1xfc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1XFC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1xfc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XFC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rcq|1rcq]], [[1sft|1sft]], [[2sfp|2sfp]], [[1bdo|1bdo]], [[1l6f|1l6f]], [[1epv|1epv]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">alr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</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=1xfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xfc OCA], [https://pdbe.org/1xfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xfc RCSB], [https://www.ebi.ac.uk/pdbsum/1xfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xfc 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=1xfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xfc OCA], [http://pdbe.org/1xfc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xfc RCSB], [http://www.ebi.ac.uk/pdbsum/1xfc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xfc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ALR_MYCTU ALR_MYCTU]] Catalyzes the interconversion of L-alanine and D-alanine.<ref>PMID:11267762</ref> | + | [https://www.uniprot.org/uniprot/ALR_MYCTU ALR_MYCTU] Catalyzes the interconversion of L-alanine and D-alanine.<ref>PMID:11267762</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: Alanine racemase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Benedik, M J]] | + | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: Briggs, J M]] | + | [[Category: Benedik MJ]] |
| - | [[Category: Ebalunode, J]] | + | [[Category: Briggs JM]] |
| - | [[Category: Im, H]] | + | [[Category: Ebalunode J]] |
| - | [[Category: Kohn, H]] | + | [[Category: Im H]] |
| - | [[Category: Krause, K L]] | + | [[Category: Kohn H]] |
| - | [[Category: LeMagueres, P]] | + | [[Category: Krause KL]] |
| - | [[Category: Strych, U]] | + | [[Category: LeMagueres P]] |
| - | [[Category: Alpha-beta barrel]]
| + | [[Category: Strych U]] |
| - | [[Category: Beta-structure for c-terminal domain]]
| + | |
| - | [[Category: Internal aldimine form]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| Structural highlights
Function
ALR_MYCTU Catalyzes the interconversion of L-alanine and D-alanine.[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
We report the crystal structure of alanine racemase from Mycobacterium tuberculosis (Alr(Mtb)) at 1.9 A resolution. In our structure, Alr(Mtb) is found to be a dimer formed by two crystallographically different monomers, each comprising 384 residues. The domain makeup of each monomer is similar to that of Bacillus and Pseudomonas alanine racemases and includes both an alpha/beta-barrel at the N-terminus and a C-terminus primarily made of beta-strands. The hinge angle between these two domains is unique for Alr(Mtb), but the active site geometry is conserved. In Alr(Mtb), the PLP cofactor is covalently bound to the protein via an internal aldimine bond with Lys42. No guest substrate is noted in its active site, although some residual electron density is observed in the enzyme's active site pocket. Analysis of the active site pocket, in the context of other known alanine racemases, allows us to propose the inclusion of conserved residues found at the entrance to the binding pocket as additional targets in ongoing structure-aided drug design efforts. Also, as observed in other alanine racemase structures, PLP adopts a conformation that significantly distorts the planarity of the extended conjugated system between the PLP ring and the internal aldimine bond.
The 1.9 A crystal structure of alanine racemase from Mycobacterium tuberculosis contains a conserved entryway into the active site.,LeMagueres P, Im H, Ebalunode J, Strych U, Benedik MJ, Briggs JM, Kohn H, Krause KL Biochemistry. 2005 Feb 8;44(5):1471-81. PMID:15683232[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Strych U, Penland RL, Jimenez M, Krause KL, Benedik MJ. Characterization of the alanine racemases from two mycobacteria. FEMS Microbiol Lett. 2001 Mar 15;196(2):93-8. PMID:11267762
- ↑ LeMagueres P, Im H, Ebalunode J, Strych U, Benedik MJ, Briggs JM, Kohn H, Krause KL. The 1.9 A crystal structure of alanine racemase from Mycobacterium tuberculosis contains a conserved entryway into the active site. Biochemistry. 2005 Feb 8;44(5):1471-81. PMID:15683232 doi:10.1021/bi0486583
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