1aw8

From Proteopedia

(Difference between revisions)

Revision as of 06:27, 11 August 2021

PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE

Structural highlights

1aw8 is a 4 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Activity:	Aspartate 1-decarboxylase, with EC number 4.1.1.11
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PAND_ECOLI] Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-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

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Cronan JE Jr. Beta-alanine synthesis in Escherichia coli. J Bacteriol. 1980 Mar;141(3):1291-7. PMID:6767707
↑ 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. Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing. Nat Struct Biol. 1998 Apr;5(4):289-93. PMID:9546220

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1aw8"

@@ Line 3: / Line 3: @@
 <StructureSection load='1aw8' size='340' side='right'caption='[[1aw8]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1aw8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AW8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1aw8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_1-decarboxylase Aspartate 1-decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.11 4.1.1.11] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aspartate_1-decarboxylase Aspartate 1-decarboxylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.11 4.1.1.11] </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=1aw8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aw8 OCA], [http://pdbe.org/1aw8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aw8 RCSB], [http://www.ebi.ac.uk/pdbsum/1aw8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1aw8 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=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 ==
-[[http://www.uniprot.org/uniprot/PAND_ECOLI PAND_ECOLI]] Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.<ref>PMID:6767707</ref>
+[[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]]

1aw8

From Proteopedia

Revision as of 06:27, 11 August 2021

PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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