1reo
From Proteopedia
(New page: 200px<br /><applet load="1reo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1reo, resolution 2.31Å" /> '''L-amino acid oxidase...) |
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| - | [[Image:1reo.jpg|left|200px]]<br /><applet load="1reo" size=" | + | [[Image:1reo.jpg|left|200px]]<br /><applet load="1reo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1reo, resolution 2.31Å" /> | caption="1reo, resolution 2.31Å" /> | ||
'''L-amino acid oxidase from Agkistrodon halys pallas'''<br /> | '''L-amino acid oxidase from Agkistrodon halys pallas'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A snake-venom protein named AHP-LAAO has been purified from Agkistrodon | + | A snake-venom protein named AHP-LAAO has been purified from Agkistrodon halys pallas venom using four-stage chromatography. AHP-LAAO is a novel member of the snake-venom L-amino-acid oxidase family. Its amino-acid sequence shows high homology to other members of this family. For L-leucine, the values of k(cat) and K(M) are 31.1 s(-1) and 0.25 mM, respectively. The molecular weight of AHP-LAAO is about 60.7 kDa as determined by MALDI-TOF mass spectrometry. AHP-LAAO can also induce apoptosis of cultured Hela cells. Two sets of diffraction data with similar resolution limits (about 2.5 A) were collected independently at MacCHESS (Cornell High Energy Synchrotron Source, USA) and IHEP (Institute of High Energy Physics, Beijing, China). The crystals belong to space group I2(1)3, with unit-cell parameter a = 169.31 A, corresponding to one molecule in the asymmetric unit and a volume-to-weight ratio of 3.33 A(3) Da(-1). The final structural model is similar to that of L-amino-acid oxidase from Calloselasma rhodostoma venom. |
==About this Structure== | ==About this Structure== | ||
| - | 1REO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gloydius_halys Gloydius halys] with NAG, NDG, CIT and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/L-amino-acid_oxidase L-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.2 1.4.3.2] Full crystallographic information is available from [http:// | + | 1REO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gloydius_halys Gloydius halys] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=NDG:'>NDG</scene>, <scene name='pdbligand=CIT:'>CIT</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/L-amino-acid_oxidase L-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.2 1.4.3.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1REO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: l-amino acid oxidase]] | [[Category: l-amino acid oxidase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:50:05 2008'' |
Revision as of 12:50, 21 February 2008
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L-amino acid oxidase from Agkistrodon halys pallas
Overview
A snake-venom protein named AHP-LAAO has been purified from Agkistrodon halys pallas venom using four-stage chromatography. AHP-LAAO is a novel member of the snake-venom L-amino-acid oxidase family. Its amino-acid sequence shows high homology to other members of this family. For L-leucine, the values of k(cat) and K(M) are 31.1 s(-1) and 0.25 mM, respectively. The molecular weight of AHP-LAAO is about 60.7 kDa as determined by MALDI-TOF mass spectrometry. AHP-LAAO can also induce apoptosis of cultured Hela cells. Two sets of diffraction data with similar resolution limits (about 2.5 A) were collected independently at MacCHESS (Cornell High Energy Synchrotron Source, USA) and IHEP (Institute of High Energy Physics, Beijing, China). The crystals belong to space group I2(1)3, with unit-cell parameter a = 169.31 A, corresponding to one molecule in the asymmetric unit and a volume-to-weight ratio of 3.33 A(3) Da(-1). The final structural model is similar to that of L-amino-acid oxidase from Calloselasma rhodostoma venom.
About this Structure
1REO is a Single protein structure of sequence from Gloydius halys with , , and as ligands. Active as L-amino-acid oxidase, with EC number 1.4.3.2 Full crystallographic information is available from OCA.
Reference
Purification, partial characterization, crystallization and structural determination of AHP-LAAO, a novel L-amino-acid oxidase with cell apoptosis-inducing activity from Agkistrodon halys pallas venom., Zhang H, Teng M, Niu L, Wang Y, Wang Y, Liu Q, Huang Q, Hao Q, Dong Y, Liu P, Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):974-7. Epub 2004, Apr 21. PMID:15103157
Page seeded by OCA on Thu Feb 21 14:50:05 2008
Categories: Gloydius halys | L-amino-acid oxidase | Single protein | Dong, Y. | Hao, Q. | Huang, Q. | Liu, P. | Liu, Q. | Niu, L. | Teng, M. | Wang, Y. | Zhang, H. | CIT | FAD | NAG | NDG | L-amino acid oxidase
