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2h3x

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Revision as of 22:01, 10 September 2015

Crystal Structure of an Electron Transfer Complex Between Aromatic Amine Dehydrogenase and Azurin from Alcaligenes Faecalis (Form 3)

Structural highlights

2h3x is a 6 chain structure with sequence from Alcaligenes faecalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	2ah1, 2h3y, 2h47
Activity:	Aralkylamine dehydrogenase (azurin), with EC number 1.4.9.2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[AAUB_ALCFA] Oxidizes primary aromatic amines and, more slowly, some long-chain aliphatic amines, but not methylamine or ethylamine. Uses azurin as an electron acceptor to transfer electrons from the reduced tryptophylquinone cofactor.^[1] ^[2] ^[3] ^[4] [AZUR_ALCFA] Transfers electrons from cytochrome c551 to cytochrome oxidase. Transfers electrons from the tryptophan tryptophylquinone of the aromatic amine dehydrogenase heterotetramer.^[5] ^[6] [AAUA_ALCFA] Oxidizes primary aromatic amines and, more slowly, some long-chain aliphatic amines, but not methylamine or ethylamine. Uses azurin as an electron acceptor to transfer electrons from the reduced tryptophylquinone cofactor.^[7] ^[8] ^[9] ^[10] ^[11] ^[12] ^[13]

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 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.

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^[14]

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

References

↑ Chistoserdov AY. Cloning, sequencing and mutagenesis of the genes for aromatic amine dehydrogenase from Alcaligenes faecalis and evolution of amine dehydrogenases. Microbiology. 2001 Aug;147(Pt 8):2195-202. PMID:11495996
↑ Hothi P, Khadra KA, Combe JP, Leys D, Scrutton NS. Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans. FEBS J. 2005 Nov;272(22):5894-909. PMID:16279953 doi:http://dx.doi.org/EJB4990
↑ Govindaraj S, Eisenstein E, Jones LH, Sanders-Loehr J, Chistoserdov AY, Davidson VL, Edwards SL. Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme. J Bacteriol. 1994 May;176(10):2922-9. PMID:8188594
↑ Masgrau L, Roujeinikova A, Johannissen LO, Hothi P, Basran J, Ranaghan KE, Mulholland AJ, Sutcliffe MJ, Scrutton NS, Leys D. Atomic description of an enzyme reaction dominated by proton tunneling. Science. 2006 Apr 14;312(5771):237-41. PMID:16614214 doi:312/5771/237
↑ Rosen P, Segal M, Pecht I. Electron transfer between azurin from Alcaligenes faecalis and cytochrome c551 from Pseudomonas aeruginosa. Eur J Biochem. 1981 Nov;120(2):339-44. PMID:6274637
↑ Sukumar N, Chen ZW, Ferrari D, Merli A, Rossi GL, Bellamy HD, Chistoserdov A, Davidson VL, Mathews FS. Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis. Biochemistry. 2006 Nov 14;45(45):13500-10. PMID:17087503 doi:http://dx.doi.org/10.1021/bi0612972
↑ Chistoserdov AY. Cloning, sequencing and mutagenesis of the genes for aromatic amine dehydrogenase from Alcaligenes faecalis and evolution of amine dehydrogenases. Microbiology. 2001 Aug;147(Pt 8):2195-202. PMID:11495996
↑ Hothi P, Khadra KA, Combe JP, Leys D, Scrutton NS. Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans. FEBS J. 2005 Nov;272(22):5894-909. PMID:16279953 doi:http://dx.doi.org/EJB4990
↑ Govindaraj S, Eisenstein E, Jones LH, Sanders-Loehr J, Chistoserdov AY, Davidson VL, Edwards SL. Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme. J Bacteriol. 1994 May;176(10):2922-9. PMID:8188594
↑ Edwards SL, Davidson VL, Hyun YL, Wingfield PT. Spectroscopic evidence for a common electron transfer pathway for two tryptophan tryptophylquinone enzymes. J Biol Chem. 1995 Mar 3;270(9):4293-8. PMID:7876189
↑ Sukumar N, Chen ZW, Ferrari D, Merli A, Rossi GL, Bellamy HD, Chistoserdov A, Davidson VL, Mathews FS. Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis. Biochemistry. 2006 Nov 14;45(45):13500-10. PMID:17087503 doi:http://dx.doi.org/10.1021/bi0612972
↑ Roujeinikova A, Scrutton NS, Leys D. Atomic level insight into the oxidative half-reaction of aromatic amine dehydrogenase. J Biol Chem. 2006 Dec 29;281(52):40264-72. Epub 2006 Sep 27. PMID:17005560 doi:http://dx.doi.org/10.1074/jbc.M605559200
↑ Masgrau L, Roujeinikova A, Johannissen LO, Hothi P, Basran J, Ranaghan KE, Mulholland AJ, Sutcliffe MJ, Scrutton NS, Leys D. Atomic description of an enzyme reaction dominated by proton tunneling. Science. 2006 Apr 14;312(5771):237-41. PMID:16614214 doi:312/5771/237
↑ Sukumar N, Chen ZW, Ferrari D, Merli A, Rossi GL, Bellamy HD, Chistoserdov A, Davidson VL, Mathews FS. Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis. Biochemistry. 2006 Nov 14;45(45):13500-10. PMID:17087503 doi:http://dx.doi.org/10.1021/bi0612972

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/2h3x"

@@ Line 6: / Line 6: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ah1|2ah1]], [[2h3y|2h3y]], [[2h47|2h47]]</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aralkylamine_dehydrogenase_(azurin) Aralkylamine dehydrogenase (azurin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.9.2 1.4.9.2] </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=2h3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h3x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2h3x RCSB], [http://www.ebi.ac.uk/pdbsum/2h3x PDBsum]</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=2h3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h3x OCA], [http://pdbe.org/2h3x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h3x RCSB], [http://www.ebi.ac.uk/pdbsum/2h3x PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2h3x" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 38: / Line 39: @@
 </StructureSection>
 [[Category: Alcaligenes faecalis]]
-[[Category: Aralkylamine dehydrogenase]]
 [[Category: Bellamy, H D]]
 [[Category: Chen, Z]]

2h3x

From Proteopedia

Revision as of 22:01, 10 September 2015

Crystal Structure of an Electron Transfer Complex Between Aromatic Amine Dehydrogenase and Azurin from Alcaligenes Faecalis (Form 3)

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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