1w2i
From Proteopedia
(New page: 200px<br /> <applet load="1w2i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w2i, resolution 1.50Å" /> '''CRYSTAL STRUCTUORE ...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1W2I is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]] with FMT as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.7 3.6.1.7]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W2I OCA]]. | + | 1W2I is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]] with FMT as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Acylphosphatase Acylphosphatase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.7 3.6.1.7]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W2I OCA]]. |
==Reference== | ==Reference== | ||
Crystal structure of a hyperthermophilic archaeal acylphosphatase from Pyrococcus horikoshii--structural insights into enzymatic catalysis, thermostability, and dimerization., Cheung YY, Lam SY, Chu WK, Allen MD, Bycroft M, Wong KB, Biochemistry. 2005 Mar 29;44(12):4601-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15779887 15779887] | Crystal structure of a hyperthermophilic archaeal acylphosphatase from Pyrococcus horikoshii--structural insights into enzymatic catalysis, thermostability, and dimerization., Cheung YY, Lam SY, Chu WK, Allen MD, Bycroft M, Wong KB, Biochemistry. 2005 Mar 29;44(12):4601-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15779887 15779887] | ||
| + | [[Category: Acylphosphatase]] | ||
[[Category: Pyrococcus horikoshii]] | [[Category: Pyrococcus horikoshii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: thermophilic]] | [[Category: thermophilic]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:33:30 2007'' |
Revision as of 11:28, 30 October 2007
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CRYSTAL STRUCTUORE OF ACYLPHOSPHATASE FROM PYROCOCCUS HORIKOSHII COMPLEXED WITH FORMATE
Overview
Acylphosphatases catalyze the hydrolysis of the carboxyl-phosphate bond in, acyl phosphates. Although acylphosphatase-like sequences are found in all, three domains of life, no structure of acylphosphatase has been reported, for bacteria and archaea so far. Here, we report the characterization of, enzymatic activities and crystal structure of an archaeal acylphosphatase., A putative acylphosphatase gene (PhAcP) was cloned from the genomic DNA of, Pyrococcus horikoshii and was expressed in Escherichia coli. Enzymatic, parameters of the recombinant PhAcP were measured using benzoyl phosphate, as the substrate. Our data suggest that, while PhAcP is less efficient, than other mammalian homologues at 25 degrees C, the thermophilic enzyme, is fully active at the optimal growth temperature (98 ... [(full description)]
About this Structure
1W2I is a [Single protein] structure of sequence from [Pyrococcus horikoshii] with FMT as [ligand]. Active as [Acylphosphatase], with EC number [3.6.1.7]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Crystal structure of a hyperthermophilic archaeal acylphosphatase from Pyrococcus horikoshii--structural insights into enzymatic catalysis, thermostability, and dimerization., Cheung YY, Lam SY, Chu WK, Allen MD, Bycroft M, Wong KB, Biochemistry. 2005 Mar 29;44(12):4601-11. PMID:15779887
Page seeded by OCA on Tue Oct 30 13:33:30 2007
Categories: Acylphosphatase | Pyrococcus horikoshii | Single protein | Allen, M.D. | Bycroft, M. | Cheung, Y.Y. | Chu, W.K. | Lam, S.Y. | Wong, K.B. | FMT | Amyloid | Phosphatase | Stability | Thermophilic
