1igb

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[[Image:1igb.gif|left|200px]]<br /><applet load="1igb" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1igb.gif|left|200px]]
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caption="1igb, resolution 2.3&Aring;" />
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'''AEROMONAS PROTEOLYTICA AMINOPEPTIDASE COMPLEXED WITH THE INHIBITOR PARA-IODO-D-PHENYLALANINE HYDROXAMATE'''<br />
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{{Structure
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|PDB= 1igb |SIZE=350|CAPTION= <scene name='initialview01'>1igb</scene>, resolution 2.3&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=IPO:PARA-IODO-D-PHENYLALANINE HYDROXAMIC ACID'>IPO</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Bacterial_leucyl_aminopeptidase Bacterial leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.10 3.4.11.10]
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|GENE=
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}}
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'''AEROMONAS PROTEOLYTICA AMINOPEPTIDASE COMPLEXED WITH THE INHIBITOR PARA-IODO-D-PHENYLALANINE HYDROXAMATE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1IGB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_proteolyticus Vibrio proteolyticus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=IPO:'>IPO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Bacterial_leucyl_aminopeptidase Bacterial leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.10 3.4.11.10] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IGB OCA].
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1IGB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_proteolyticus Vibrio proteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IGB OCA].
==Reference==
==Reference==
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The structure of the Aeromonas proteolytica aminopeptidase complexed with a hydroxamate inhibitor. Involvement in catalysis of Glu151 and two zinc ions of the co-catalytic unit., Chevrier B, D'Orchymont H, Schalk C, Tarnus C, Moras D, Eur J Biochem. 1996 Apr 15;237(2):393-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8647077 8647077]
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The structure of the Aeromonas proteolytica aminopeptidase complexed with a hydroxamate inhibitor. Involvement in catalysis of Glu151 and two zinc ions of the co-catalytic unit., Chevrier B, D'Orchymont H, Schalk C, Tarnus C, Moras D, Eur J Biochem. 1996 Apr 15;237(2):393-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8647077 8647077]
[[Category: Bacterial leucyl aminopeptidase]]
[[Category: Bacterial leucyl aminopeptidase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:50:00 2008''

Revision as of 09:50, 20 March 2008


PDB ID 1igb

Drag the structure with the mouse to rotate
, resolution 2.3Å
Ligands: and
Activity: Bacterial leucyl aminopeptidase, with EC number 3.4.11.10
Coordinates: save as pdb, mmCIF, xml



AEROMONAS PROTEOLYTICA AMINOPEPTIDASE COMPLEXED WITH THE INHIBITOR PARA-IODO-D-PHENYLALANINE HYDROXAMATE


Overview

The structure of the complex of Aeromonas proteolytica aminopeptidase, a two-zinc exopeptidase, with the inhibitor p-iodo-D-phenylalanine hydroxamate has been determined by X-ray crystallography. Refinement of the structure, which includes 220 water molecules, using data at 0.80-0.23-nm resolution resulted in a crystallographic residual R value of 16%. The hydroxamate group adopts a planar conformation whereby the two oxygen atoms interact with the zinc ions. The N-hydroxyl group of the inhibitor is located between the two zinc ions, a position which is close to that occupied by a water molecule in the native structure. The carbonyl oxygen of the inhibitor binds to Zn1, which becomes pentacoordinated while Zn2 remains tetracoordinated, in contrast to the native protein where both zinc ions were shown to be tetracoordinated and structurally equivalent. Interactions of the carboxylate oxygens of Glu151 with the hydroxamate group play an important role in the stabilization of the complex.

About this Structure

1IGB is a Single protein structure of sequence from Vibrio proteolyticus. Full crystallographic information is available from OCA.

Reference

The structure of the Aeromonas proteolytica aminopeptidase complexed with a hydroxamate inhibitor. Involvement in catalysis of Glu151 and two zinc ions of the co-catalytic unit., Chevrier B, D'Orchymont H, Schalk C, Tarnus C, Moras D, Eur J Biochem. 1996 Apr 15;237(2):393-8. PMID:8647077

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