1aw8
From Proteopedia
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- | [[Image:1aw8.png|left|200px]] | ||
- | < | + | ==PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE== |
- | + | <StructureSection load='1aw8' size='340' side='right'caption='[[1aw8]], [[Resolution|resolution]] 2.20Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[1aw8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AW8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AW8 FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | |
- | - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></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=1aw8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aw8 OCA], [https://pdbe.org/1aw8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aw8 RCSB], [https://www.ebi.ac.uk/pdbsum/1aw8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aw8 ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/PAND_ECOLI PAND_ECOLI] Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.<ref>PMID:6767707</ref> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aw/1aw8_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1aw8 ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The structure of L-aspartate-alpha-decarboxylase from E. coli has been determined at 2.2 A resolution. The enzyme is a tetramer with pseudofour-fold rotational symmetry. The subunits are six-stranded beta-barrels capped by small alpha-helices at each end. The active sites are located between adjacent subunits. The electron density provides evidence for catalytic pyruvoyl groups at three active sites and an ester at the fourth. The ester is an intermediate in the autocatalytic self-processing leading to formation of the pyruvoyl group. This unprecedented structure provides novel insights into the general phenomenon of protein processing. | ||
- | + | Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing.,Albert A, Dhanaraj V, Genschel U, Khan G, Ramjee MK, Pulido R, Sibanda BL, von Delft F, Witty M, Blundell TL, Smith AG, Abell C Nat Struct Biol. 1998 Apr;5(4):289-93. PMID:9546220<ref>PMID:9546220</ref> | |
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 1aw8" style="background-color:#fffaf0;"></div> | ||
- | + | ==See Also== | |
- | + | *[[Aspartate decarboxylase 3D structures|Aspartate decarboxylase 3D structures]] | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | |
- | [[ | + | |
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- | == | + | |
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
- | [[Category: Abell | + | [[Category: Large Structures]] |
- | [[Category: Albert | + | [[Category: Abell C]] |
- | [[Category: Blundell | + | [[Category: Albert A]] |
- | [[Category: Dhanaraj | + | [[Category: Blundell TL]] |
- | [[Category: Genschel | + | [[Category: Dhanaraj V]] |
- | [[Category: Khan | + | [[Category: Genschel U]] |
- | [[Category: Pulido | + | [[Category: Khan G]] |
- | [[Category: Ramjee | + | [[Category: Pulido R]] |
- | [[Category: Smith | + | [[Category: Ramjee MK]] |
- | [[Category: Sybanda | + | [[Category: Smith AG]] |
- | + | [[Category: Sybanda BL]] | |
- | [[Category: Witty | + | [[Category: Witty M]] |
- | [[Category: | + | [[Category: Von Delf F]] |
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Current revision
PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE
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Categories: Escherichia coli | Large Structures | Abell C | Albert A | Blundell TL | Dhanaraj V | Genschel U | Khan G | Pulido R | Ramjee MK | Smith AG | Sybanda BL | Witty M | Von Delf F