2iaa

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[[Image:2iaa.gif|left|200px]]<br /><applet load="2iaa" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2iaa.gif|left|200px]]
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caption="2iaa, resolution 1.95&Aring;" />
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'''Crystal Structure of an Electron Transfer Complex Between Aromatic Amine Dephydrogenase and Azurin from Alcaligenes Faecalis (Form 2)'''<br />
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{{Structure
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|PDB= 2iaa |SIZE=350|CAPTION= <scene name='initialview01'>2iaa</scene>, resolution 1.95&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CU:COPPER (II) ION'>CU</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Aralkylamine_dehydrogenase Aralkylamine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.99.4 1.4.99.4]
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|GENE=
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}}
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'''Crystal Structure of an Electron Transfer Complex Between Aromatic Amine Dephydrogenase and Azurin from Alcaligenes Faecalis (Form 2)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2IAA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis] with <scene name='pdbligand=CU:'>CU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Aralkylamine_dehydrogenase Aralkylamine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.99.4 1.4.99.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IAA OCA].
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2IAA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IAA OCA].
==Reference==
==Reference==
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Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis., Sukumar N, Chen ZW, Ferrari D, Merli A, Rossi GL, Bellamy HD, Chistoserdov A, Davidson VL, Mathews FS, Biochemistry. 2006 Nov 14;45(45):13500-10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17087503 17087503]
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Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis., Sukumar N, Chen ZW, Ferrari D, Merli A, Rossi GL, Bellamy HD, Chistoserdov A, Davidson VL, Mathews FS, Biochemistry. 2006 Nov 14;45(45):13500-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17087503 17087503]
[[Category: Alcaligenes faecalis]]
[[Category: Alcaligenes faecalis]]
[[Category: Aralkylamine dehydrogenase]]
[[Category: Aralkylamine dehydrogenase]]
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[[Category: tryptophan tryptophylquinone]]
[[Category: tryptophan tryptophylquinone]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:50:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:27:06 2008''

Revision as of 15:27, 20 March 2008

Image:2iaa.gif


PDB ID 2iaa

Drag the structure with the mouse to rotate
, resolution 1.95Å
Ligands:
Activity: Aralkylamine dehydrogenase, with EC number 1.4.99.4
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of an Electron Transfer Complex Between Aromatic Amine Dephydrogenase and Azurin from Alcaligenes Faecalis (Form 2)


Overview

The crystal structure of an electron transfer complex of aromatic amine dehydrogenase (AADH) and azurin is presented. Electrons are transferred from the tryptophan tryptophylquinone (TTQ) cofactor of AADH to the type I copper of the cupredoxin azurin. This structure is compared with the complex of the TTQ-containing methylamine dehydrogenase (MADH) and the cupredoxin amicyanin. Despite significant similarities between the two quinoproteins and the two cupredoxins, each is specific for its respective partner and the ionic strength dependence and magnitude of the binding constant for each complex are quite different. The AADH-azurin interface is largely hydrophobic, covering approximately 500 A(2) of surface on each molecule, with one direct hydrogen bond linking them. The closest distance from TTQ to copper is 12.6 A compared with a distance of 9.3 A in the MADH-amicyanin complex. When the MADH-amicyanin complex is aligned with the AADH-azurin complex, the amicyanin lies on top of the azurin but is oriented quite differently. Although the copper atoms differ in position by approximately 4.7 A, the amicyanin bound to MADH appears to be rotated approximately 90 degrees from its aligned position with azurin. Comparison of the structures of the two complexes identifies features of the interface that dictate the specificity of the protein-protein interaction and determine the rate of interprotein electron transfer.

About this Structure

2IAA is a Single protein structure of sequence from Alcaligenes faecalis. Full crystallographic information is available from OCA.

Reference

Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis., Sukumar N, Chen ZW, Ferrari D, Merli A, Rossi GL, Bellamy HD, Chistoserdov A, Davidson VL, Mathews FS, Biochemistry. 2006 Nov 14;45(45):13500-10. PMID:17087503

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