1aw8
From Proteopedia
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| - | [[Image:1aw8.gif|left|200px]]<br /><applet load="1aw8" size=" | + | [[Image:1aw8.gif|left|200px]]<br /><applet load="1aw8" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1aw8, resolution 2.2Å" /> | caption="1aw8, resolution 2.2Å" /> | ||
'''PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE'''<br /> | '''PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AW8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [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] Known structural/functional Site: <scene name='pdbsite=NUL:Pvl Residues'>NUL</scene>. Full crystallographic information is available from [http:// | + | 1AW8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [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] Known structural/functional Site: <scene name='pdbsite=NUL:Pvl+Residues'>NUL</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AW8 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: protein self-processing]] | [[Category: protein self-processing]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:31:51 2008'' |
Revision as of 07:31, 3 February 2008
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PYRUVOYL DEPENDENT ASPARTATE DECARBOXYLASE
Overview
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.
About this Structure
1AW8 is a Protein complex structure of sequences from Escherichia coli. Active as Aspartate 1-decarboxylase, with EC number 4.1.1.11 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Feb 3 09:31:51 2008
Categories: Aspartate 1-decarboxylase | Escherichia coli | Protein complex | Abell, C. | Albert, A. | Blundell, T.L. | Dhanaraj, V. | Genschel, U. | Khan, G. | Pulido, R. | Ramjee, M.K. | Smith, A.G. | Sybanda, B.L. | Vondelf, F. | Witty, M. | Decarboxylase | Lyase | Pantothenate pathway | Protein self-processing
