1jkm

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(New page: 200px<br /><applet load="1jkm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jkm, resolution 1.85&Aring;" /> '''BREFELDIN A ESTERASE...)
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[[Image:1jkm.gif|left|200px]]<br /><applet load="1jkm" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jkm.gif|left|200px]]<br /><applet load="1jkm" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jkm, resolution 1.85&Aring;" />
caption="1jkm, resolution 1.85&Aring;" />
'''BREFELDIN A ESTERASE, A BACTERIAL HOMOLOGUE OF HUMAN HORMONE SENSITIVE LIPASE'''<br />
'''BREFELDIN A ESTERASE, A BACTERIAL HOMOLOGUE OF HUMAN HORMONE SENSITIVE LIPASE'''<br />
==Overview==
==Overview==
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Brefeldin A esterase (BFAE), a detoxifying enzyme isolated from Bacillus, subtilis, hydrolyzes and inactivates BFA, a potent fungal inhibitor of, intracellular vesicle-dependent secretory transport and poliovirus RNA, replication. We have solved the crystal structure of BFAE and we, discovered that the previously reported amino acid sequence was in serious, error due to frame shifts in the cDNA sequence. The correct sequence, inferred from the experimentally phased electron density map, revealed, that BFAE is a homolog of the mammalian hormone sensitive lipase (HSL). It, is a canonical alpha/beta hydrolase with two insertions forming the, substrate binding pocket. The enzyme contains a lipase-like catalytic, triad, Ser 202, Asp 308 and His 338, consistent with mutational studies, that implicate the homologous Ser 424, Asp 693 and His 723 in the, catalytic triad in human HSL.
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Brefeldin A esterase (BFAE), a detoxifying enzyme isolated from Bacillus subtilis, hydrolyzes and inactivates BFA, a potent fungal inhibitor of intracellular vesicle-dependent secretory transport and poliovirus RNA replication. We have solved the crystal structure of BFAE and we discovered that the previously reported amino acid sequence was in serious error due to frame shifts in the cDNA sequence. The correct sequence, inferred from the experimentally phased electron density map, revealed that BFAE is a homolog of the mammalian hormone sensitive lipase (HSL). It is a canonical alpha/beta hydrolase with two insertions forming the substrate binding pocket. The enzyme contains a lipase-like catalytic triad, Ser 202, Asp 308 and His 338, consistent with mutational studies that implicate the homologous Ser 424, Asp 693 and His 723 in the catalytic triad in human HSL.
==About this Structure==
==About this Structure==
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1JKM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JKM OCA].
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1JKM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JKM OCA].
==Reference==
==Reference==
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Contreras, A.J.]]
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[[Category: Contreras, A J.]]
[[Category: Derewenda, U.]]
[[Category: Derewenda, U.]]
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[[Category: Derewenda, Z.S.]]
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[[Category: Derewenda, Z S.]]
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[[Category: Matern, U.O.]]
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[[Category: Matern, U O.]]
[[Category: Osterlund, T.]]
[[Category: Osterlund, T.]]
[[Category: Sheffield, P.]]
[[Category: Sheffield, P.]]
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[[Category: serine hydrolase]]
[[Category: serine hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:47:37 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:23:42 2008''

Revision as of 11:23, 21 February 2008


1jkm, resolution 1.85Å

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BREFELDIN A ESTERASE, A BACTERIAL HOMOLOGUE OF HUMAN HORMONE SENSITIVE LIPASE

Overview

Brefeldin A esterase (BFAE), a detoxifying enzyme isolated from Bacillus subtilis, hydrolyzes and inactivates BFA, a potent fungal inhibitor of intracellular vesicle-dependent secretory transport and poliovirus RNA replication. We have solved the crystal structure of BFAE and we discovered that the previously reported amino acid sequence was in serious error due to frame shifts in the cDNA sequence. The correct sequence, inferred from the experimentally phased electron density map, revealed that BFAE is a homolog of the mammalian hormone sensitive lipase (HSL). It is a canonical alpha/beta hydrolase with two insertions forming the substrate binding pocket. The enzyme contains a lipase-like catalytic triad, Ser 202, Asp 308 and His 338, consistent with mutational studies that implicate the homologous Ser 424, Asp 693 and His 723 in the catalytic triad in human HSL.

About this Structure

1JKM is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Crystal structure of brefeldin A esterase, a bacterial homolog of the mammalian hormone-sensitive lipase., Wei Y, Contreras JA, Sheffield P, Osterlund T, Derewenda U, Kneusel RE, Matern U, Holm C, Derewenda ZS, Nat Struct Biol. 1999 Apr;6(4):340-5. PMID:10201402

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