2bfw
From Proteopedia
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| - | [[Image:2bfw.gif|left|200px]]<br /><applet load="2bfw" size=" | + | [[Image:2bfw.gif|left|200px]]<br /><applet load="2bfw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2bfw, resolution 1.80Å" /> | caption="2bfw, resolution 1.80Å" /> | ||
'''STRUCTURE OF THE C DOMAIN OF GLYCOGEN SYNTHASE FROM PYROCOCCUS ABYSSI'''<br /> | '''STRUCTURE OF THE C DOMAIN OF GLYCOGEN SYNTHASE FROM PYROCOCCUS ABYSSI'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BFW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi] with SO4 and ACT as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Starch_synthase Starch synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.21 2.4.1.21] Known structural/functional Site: <scene name='pdbsite=AC1:Act Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2BFW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Starch_synthase Starch synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.21 2.4.1.21] Known structural/functional Site: <scene name='pdbsite=AC1:Act+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:23:36 2008'' |
Revision as of 08:23, 3 February 2008
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STRUCTURE OF THE C DOMAIN OF GLYCOGEN SYNTHASE FROM PYROCOCCUS ABYSSI
Overview
Glycogen and starch synthases are retaining glycosyltransferases that, catalyze the transfer of glucosyl residues to the non-reducing end of a, growing alpha-1,4-glucan chain, a central process of the carbon/energy, metabolism present in almost all living organisms. The crystal structure, of the glycogen synthase from Pyrococcus abyssi, the smallest known member, of this family of enzymes, revealed that its subunits possess a fold, common to other glycosyltransferases, a pair of beta/alpha/beta Rossmann, fold-type domains with the catalytic site at their interface., Nevertheless, the archaeal enzyme presents an unprecedented homotrimeric, molecular arrangement both in solution, as determined by analytical, ultracentrifugation, and in the crystal. The C-domains are not involved in, intersubunit interactions of the trimeric molecule, thus allowing for, movements, likely required for catalysis, across the narrow hinge that, connects the N- and C-domains. The radial disposition of the subunits, confers on the molecule a distinct triangular shape, clearly visible with, negative staining electron microscopy, in which the upper and lower faces, present a sharp asymmetry. Comparison of bacterial and eukaryotic glycogen, synthases, which use, respectively, ADP or UDP glucose as donor, substrates, with the archaeal enzyme, which can utilize both molecules, allowed us to propose the residues that determine glucosyl donor, specificity.
About this Structure
2BFW is a Single protein structure of sequence from Pyrococcus abyssi with and as ligands. Active as Starch synthase, with EC number 2.4.1.21 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure of an archaeal glycogen synthase: insights into oligomerization and substrate binding of eukaryotic glycogen synthases., Horcajada C, Guinovart JJ, Fita I, Ferrer JC, J Biol Chem. 2006 Feb 3;281(5):2923-31. Epub 2005 Nov 29. PMID:16319074
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