1lf9

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[[Image:1lf9.gif|left|200px]]<br /><applet load="1lf9" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1lf9.gif|left|200px]]
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caption="1lf9, resolution 2.20&Aring;" />
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'''CRYSTAL STRUCTURE OF BACTERIAL GLUCOAMYLASE COMPLEXED WITH ACARBOSE'''<br />
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{{Structure
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|PDB= 1lf9 |SIZE=350|CAPTION= <scene name='initialview01'>1lf9</scene>, resolution 2.20&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ACR:ACARBOSE'>ACR</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF BACTERIAL GLUCOAMYLASE COMPLEXED WITH ACARBOSE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1LF9 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=ACR:'>ACR</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1LF9 OCA].
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1LF9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermoanaerobacterium_thermosaccharolyticum Thermoanaerobacterium thermosaccharolyticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LF9 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12614608 12614608]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12614608 12614608]
[[Category: Glucan 1,4-alpha-glucosidase]]
[[Category: Glucan 1,4-alpha-glucosidase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: super beta sandwich]]
[[Category: super beta sandwich]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:44:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:30:15 2008''

Revision as of 10:30, 20 March 2008


PDB ID 1lf9

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands: and
Activity: Glucan 1,4-alpha-glucosidase, with EC number 3.2.1.3
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF BACTERIAL GLUCOAMYLASE COMPLEXED WITH ACARBOSE


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

1LF9 is a Single protein structure of sequence from Thermoanaerobacterium thermosaccharolyticum. 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

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