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1pt0

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[[Image:1pt0.jpg|left|200px]]<br /><applet load="1pt0" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1pt0.jpg|left|200px]]
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caption="1pt0, resolution 2.00&Aring;" />
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'''Unprocessed Pyruvoyl Dependent Aspartate Decarboxylase with an Alanine insertion at position 26'''<br />
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{{Structure
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|PDB= 1pt0 |SIZE=350|CAPTION= <scene name='initialview01'>1pt0</scene>, resolution 2.00&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|ACTIVITY= [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]
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|GENE= PAND ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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}}
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'''Unprocessed Pyruvoyl Dependent Aspartate Decarboxylase with an Alanine insertion at position 26'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1PT0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PT0 OCA].
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1PT0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PT0 OCA].
==Reference==
==Reference==
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Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase., Schmitzberger F, Kilkenny ML, Lobley CM, Webb ME, Vinkovic M, Matak-Vinkovic D, Witty M, Chirgadze DY, Smith AG, Abell C, Blundell TL, EMBO J. 2003 Dec 1;22(23):6193-204. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14633979 14633979]
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Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase., Schmitzberger F, Kilkenny ML, Lobley CM, Webb ME, Vinkovic M, Matak-Vinkovic D, Witty M, Chirgadze DY, Smith AG, Abell C, Blundell TL, EMBO J. 2003 Dec 1;22(23):6193-204. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14633979 14633979]
[[Category: Aspartate 1-decarboxylase]]
[[Category: Aspartate 1-decarboxylase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: protein self-processing]]
[[Category: protein self-processing]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:28:37 2008''

Revision as of 11:28, 20 March 2008

Image:1pt0.jpg


PDB ID 1pt0

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands:
Gene: PAND (Escherichia coli)
Activity: Aspartate 1-decarboxylase, with EC number 4.1.1.11
Coordinates: save as pdb, mmCIF, xml



Unprocessed Pyruvoyl Dependent Aspartate Decarboxylase with an Alanine insertion at position 26


Overview

Aspartate decarboxylase, which is translated as a pro-protein, undergoes intramolecular self-cleavage at Gly24-Ser25. We have determined the crystal structures of an unprocessed native precursor, in addition to Ala24 insertion, Ala26 insertion and Gly24-->Ser, His11-->Ala, Ser25-->Ala, Ser25-->Cys and Ser25-->Thr mutants. Comparative analyses of the cleavage site reveal specific conformational constraints that govern self-processing and demonstrate that considerable rearrangement must occur. We suggest that Thr57 Ogamma and a water molecule form an 'oxyanion hole' that likely stabilizes the proposed oxyoxazolidine intermediate. Thr57 and this water molecule are probable catalytic residues able to support acid-base catalysis. The conformational freedom in the loop preceding the cleavage site appears to play a determining role in the reaction. The molecular mechanism of self-processing, presented here, emphasizes the importance of stabilization of the oxyoxazolidine intermediate. Comparison of the structural features shows significant similarity to those in other self-processing systems, and suggests that models of the cleavage site of such enzymes based on Ser-->Ala or Ser-->Thr mutants alone may lead to erroneous interpretations of the mechanism.

About this Structure

1PT0 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase., Schmitzberger F, Kilkenny ML, Lobley CM, Webb ME, Vinkovic M, Matak-Vinkovic D, Witty M, Chirgadze DY, Smith AG, Abell C, Blundell TL, EMBO J. 2003 Dec 1;22(23):6193-204. PMID:14633979

Page seeded by OCA on Thu Mar 20 13:28:37 2008

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