1g5a

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|PDB= 1g5a |SIZE=350|CAPTION= <scene name='initialview01'>1g5a</scene>, resolution 1.40&Aring;
|PDB= 1g5a |SIZE=350|CAPTION= <scene name='initialview01'>1g5a</scene>, resolution 1.40&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> and <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID'>EPE</scene>
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|LIGAND= <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Amylosucrase Amylosucrase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.4 2.4.1.4]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Amylosucrase Amylosucrase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.4 2.4.1.4] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g5a OCA], [http://www.ebi.ac.uk/pdbsum/1g5a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g5a RCSB]</span>
}}
}}
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[[Category: Skov, L K.]]
[[Category: Skov, L K.]]
[[Category: Willemot, R M.]]
[[Category: Willemot, R M.]]
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[[Category: EPE]]
 
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[[Category: NA]]
 
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[[Category: TRS]]
 
[[Category: (beta-alpha)8 barrel]]
[[Category: (beta-alpha)8 barrel]]
[[Category: glycoside hydrolase]]
[[Category: glycoside hydrolase]]
[[Category: glycosyltransferase]]
[[Category: glycosyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:18:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:36:54 2008''

Revision as of 17:36, 30 March 2008


PDB ID 1g5a

Drag the structure with the mouse to rotate
, resolution 1.40Å
Ligands: , ,
Activity: Amylosucrase, with EC number 2.4.1.4
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



AMYLOSUCRASE FROM NEISSERIA POLYSACCHAREA


Overview

Amylosucrase (E.C. 2.4.1.4) is a member of Family 13 of the glycoside hydrolases (the alpha-amylases), although its biological function is the synthesis of amylose-like polymers from sucrose. The structure of amylosucrase from Neisseria polysaccharea is divided into five domains: an all helical N-terminal domain that is not similar to any known fold, a (beta/alpha)(8)-barrel A-domain, B- and B'-domains displaying alpha/beta-structure, and a C-terminal eight-stranded beta-sheet domain. In contrast to other Family 13 hydrolases that have the active site in the bottom of a large cleft, the active site of amylosucrase is at the bottom of a pocket at the molecular surface. A substrate binding site resembling the amylase 2 subsite is not found in amylosucrase. The site is blocked by a salt bridge between residues in the second and eight loops of the (beta/alpha)(8)-barrel. The result is an exo-acting enzyme. Loop 7 in the amylosucrase barrel is prolonged compared with the loop structure found in other hydrolases, and this insertion (forming domain B') is suggested to be important for the polymer synthase activity of the enzyme. The topology of the B'-domain creates an active site entrance with several ravines in the molecular surface that could be used specifically by the substrates/products (sucrose, glucan polymer, and fructose) that have to get in and out of the active site pocket.

About this Structure

1G5A is a Single protein structure of sequence from Neisseria polysaccharea. Full crystallographic information is available from OCA.

Reference

Amylosucrase, a glucan-synthesizing enzyme from the alpha-amylase family., Skov LK, Mirza O, Henriksen A, De Montalk GP, Remaud-Simeon M, Sarcabal P, Willemot RM, Monsan P, Gajhede M, J Biol Chem. 2001 Jul 6;276(27):25273-8. Epub 2001 Apr 16. PMID:11306569

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