1tu5
From Proteopedia
(New page: 200px<br /><applet load="1tu5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tu5, resolution 2.37Å" /> '''Crystal structure of...) |
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| - | [[Image:1tu5.gif|left|200px]]<br /><applet load="1tu5" size=" | + | [[Image:1tu5.gif|left|200px]]<br /><applet load="1tu5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tu5, resolution 2.37Å" /> | caption="1tu5, resolution 2.37Å" /> | ||
'''Crystal structure of bovine plasma copper-containing amine oxidase'''<br /> | '''Crystal structure of bovine plasma copper-containing amine oxidase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Copper-containing amine oxidase extracted from bovine serum (BSAO) was | + | Copper-containing amine oxidase extracted from bovine serum (BSAO) was crystallized and its three-dimensional structure at 2.37A resolution is described. The biological unit of BSAO is a homodimer, formed by two monomers related to each other by a non-crystallographic 2-fold axis. Each monomer is composed of three domains, similar to those of other amine oxidases from lower species. The two monomers are structurally equivalent, despite some minor differences at the two active sites. A large funnel allows access of substrates to the active-site; another cavity, accessible to the solvent, is also present between the two monomers; this second cavity could allow the entrance of molecular oxygen necessary for the oxidative reaction. Some sugar residues, bound to Asn, were still present and visible in the electron density map, in spite of the exhaustive deglycosylation necessary to grow the crystals. The comparison of the BSAO structure with those of other resolved AO structures shows strong dissimilarities in the architecture and charge distribution of the cavities leading to the active-site, possibly explaining the differences in substrate specificity. |
==About this Structure== | ==About this Structure== | ||
| - | 1TU5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with NAG, NDG, CU, CA and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Amine_oxidase_(copper-containing) Amine oxidase (copper-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.6 1.4.3.6] Full crystallographic information is available from [http:// | + | 1TU5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=NDG:'>NDG</scene>, <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Amine_oxidase_(copper-containing) Amine oxidase (copper-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.6 1.4.3.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TU5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Calderone, V.]] | [[Category: Calderone, V.]] | ||
[[Category: Lunelli, M.]] | [[Category: Lunelli, M.]] | ||
| - | [[Category: Paolo, M | + | [[Category: Paolo, M L.Di.]] |
[[Category: Rigo, A.]] | [[Category: Rigo, A.]] | ||
[[Category: Scarpa, M.]] | [[Category: Scarpa, M.]] | ||
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[[Category: tpq]] | [[Category: tpq]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:17:21 2008'' |
Revision as of 13:17, 21 February 2008
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Crystal structure of bovine plasma copper-containing amine oxidase
Overview
Copper-containing amine oxidase extracted from bovine serum (BSAO) was crystallized and its three-dimensional structure at 2.37A resolution is described. The biological unit of BSAO is a homodimer, formed by two monomers related to each other by a non-crystallographic 2-fold axis. Each monomer is composed of three domains, similar to those of other amine oxidases from lower species. The two monomers are structurally equivalent, despite some minor differences at the two active sites. A large funnel allows access of substrates to the active-site; another cavity, accessible to the solvent, is also present between the two monomers; this second cavity could allow the entrance of molecular oxygen necessary for the oxidative reaction. Some sugar residues, bound to Asn, were still present and visible in the electron density map, in spite of the exhaustive deglycosylation necessary to grow the crystals. The comparison of the BSAO structure with those of other resolved AO structures shows strong dissimilarities in the architecture and charge distribution of the cavities leading to the active-site, possibly explaining the differences in substrate specificity.
About this Structure
1TU5 is a Single protein structure of sequence from Bos taurus with , , , and as ligands. Active as Amine oxidase (copper-containing), with EC number 1.4.3.6 Full crystallographic information is available from OCA.
Reference
Crystal structure of amine oxidase from bovine serum., Lunelli M, Di Paolo ML, Biadene M, Calderone V, Battistutta R, Scarpa M, Rigo A, Zanotti G, J Mol Biol. 2005 Mar 4;346(4):991-1004. Epub 2005 Jan 25. PMID:15701511
Page seeded by OCA on Thu Feb 21 15:17:21 2008
Categories: Amine oxidase (copper-containing) | Bos taurus | Single protein | Battistutta, R. | Biadene, M. | Calderone, V. | Lunelli, M. | Paolo, M L.Di. | Rigo, A. | Scarpa, M. | Zanotti, G. | CA | CL | CU | NAG | NDG | Amine oxidase | Copper | Oxidoreductase | Quinoenzyme | Tpq
