1lf6

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(New page: 200px<br /><applet load="1lf6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lf6, resolution 2.10&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1lf6.gif|left|200px]]<br /><applet load="1lf6" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1lf6.gif|left|200px]]<br /><applet load="1lf6" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1lf6, resolution 2.10&Aring;" />
caption="1lf6, resolution 2.10&Aring;" />
'''CRYSTAL STRUCTURE OF BACTERIAL GLUCOAMYLASE'''<br />
'''CRYSTAL STRUCTURE OF BACTERIAL GLUCOAMYLASE'''<br />
==Overview==
==Overview==
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The first crystal structures of a two-domain, prokaryotic glucoamylase, were determined to high resolution from the clostridial species, Thermoanaerobacterium thermosaccharolyticum with and without acarbose. The, N-terminal domain has 18 antiparallel strands arranged in beta-sheets of a, super-beta-sandwich. The C-terminal domain is an (alpha/alpha)(6) barrel, lacking the peripheral subdomain of eukaryotic glucoamylases. Interdomain, contacts are common to all prokaryotic Family GH15 proteins. Domains, similar to those of prokaryotic glucoamylases in maltose phosphorylases, (Family GH65) and glycoaminoglycan lyases (Family PL8) suggest evolution, from a common ancestor. Eukaryotic glucoamylases may have evolved from, prokaryotic glucoamylases by the substitution of the N-terminal domain, with the peripheral subdomain and by the addition of a starch-binding, domain.
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The first crystal structures of a two-domain, prokaryotic glucoamylase were determined to high resolution from the clostridial species Thermoanaerobacterium thermosaccharolyticum with and without acarbose. The N-terminal domain has 18 antiparallel strands arranged in beta-sheets of a super-beta-sandwich. The C-terminal domain is an (alpha/alpha)(6) barrel, lacking the peripheral subdomain of eukaryotic glucoamylases. Interdomain contacts are common to all prokaryotic Family GH15 proteins. Domains similar to those of prokaryotic glucoamylases in maltose phosphorylases (Family GH65) and glycoaminoglycan lyases (Family PL8) suggest evolution from a common ancestor. Eukaryotic glucoamylases may have evolved from prokaryotic glucoamylases by the substitution of the N-terminal domain with the peripheral subdomain and by the addition of a starch-binding domain.
==About this Structure==
==About this Structure==
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1LF6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoanaerobacterium_thermosaccharolyticum Thermoanaerobacterium thermosaccharolyticum] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glucan_1,4-alpha-glucosidase Glucan 1,4-alpha-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.3 3.2.1.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LF6 OCA].
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1LF6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoanaerobacterium_thermosaccharolyticum Thermoanaerobacterium thermosaccharolyticum] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glucan_1,4-alpha-glucosidase Glucan 1,4-alpha-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.3 3.2.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LF6 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermoanaerobacterium thermosaccharolyticum]]
[[Category: Thermoanaerobacterium thermosaccharolyticum]]
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[[Category: Aleshin, A.E.]]
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[[Category: Aleshin, A E.]]
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[[Category: Feng, P.H.]]
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[[Category: Feng, P H.]]
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[[Category: Honzatko, R.B.]]
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[[Category: Honzatko, R B.]]
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[[Category: Reilly, P.J.]]
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[[Category: Reilly, P J.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: (alpha/alpha) barrel]]
[[Category: (alpha/alpha) barrel]]
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[[Category: super beta sandwich]]
[[Category: super beta sandwich]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:54:49 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:44:26 2008''

Revision as of 11:44, 21 February 2008


1lf6, resolution 2.10Å

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CRYSTAL STRUCTURE OF BACTERIAL GLUCOAMYLASE

Overview

The first crystal structures of a two-domain, prokaryotic glucoamylase were determined to high resolution from the clostridial species Thermoanaerobacterium thermosaccharolyticum with and without acarbose. The N-terminal domain has 18 antiparallel strands arranged in beta-sheets of a super-beta-sandwich. The C-terminal domain is an (alpha/alpha)(6) barrel, lacking the peripheral subdomain of eukaryotic glucoamylases. Interdomain contacts are common to all prokaryotic Family GH15 proteins. Domains similar to those of prokaryotic glucoamylases in maltose phosphorylases (Family GH65) and glycoaminoglycan lyases (Family PL8) suggest evolution from a common ancestor. Eukaryotic glucoamylases may have evolved from prokaryotic glucoamylases by the substitution of the N-terminal domain with the peripheral subdomain and by the addition of a starch-binding domain.

About this Structure

1LF6 is a Single protein structure of sequence from Thermoanaerobacterium thermosaccharolyticum with as ligand. Active as Glucan 1,4-alpha-glucosidase, with EC number 3.2.1.3 Full crystallographic information is available from OCA.

Reference

Crystal structure and evolution of a prokaryotic glucoamylase., Aleshin AE, Feng PH, Honzatko RB, Reilly PJ, J Mol Biol. 2003 Mar 14;327(1):61-73. PMID:12614608

Page seeded by OCA on Thu Feb 21 13:44:26 2008

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