1s2o

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|PDB= 1s2o |SIZE=350|CAPTION= <scene name='initialview01'>1s2o</scene>, resolution 1.4&Aring;
|PDB= 1s2o |SIZE=350|CAPTION= <scene name='initialview01'>1s2o</scene>, resolution 1.4&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Sucrose-phosphatase Sucrose-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.24 3.1.3.24]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Sucrose-phosphatase Sucrose-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.24 3.1.3.24] </span>
|GENE= spp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Synechocystis sp.])
|GENE= spp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1143 Synechocystis sp.])
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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=1s2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s2o OCA], [http://www.ebi.ac.uk/pdbsum/1s2o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1s2o RCSB]</span>
}}
}}
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[[Category: Fieulaine, S.]]
[[Category: Fieulaine, S.]]
[[Category: Lunn, J E.]]
[[Category: Lunn, J E.]]
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[[Category: MG]]
 
[[Category: cyanobacteria]]
[[Category: cyanobacteria]]
[[Category: had superfamily]]
[[Category: had superfamily]]
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[[Category: sucrose]]
[[Category: sucrose]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:59:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:36:32 2008''

Revision as of 20:36, 30 March 2008


PDB ID 1s2o

Drag the structure with the mouse to rotate
, resolution 1.4Å
Ligands:
Gene: spp (Synechocystis sp.)
Activity: Sucrose-phosphatase, with EC number 3.1.3.24
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



X-Ray structure of the sucrose-phosphatase (SPP) from Synechocystis sp. PCC6803 at 1.40 A resolution


Overview

Sucrose-phosphatase (SPP) catalyzes the final step in the pathway of sucrose biosynthesis in both plants and cyanobacteria, and the SPPs from these two groups of organisms are closely related. We have crystallized the enzyme from the cyanobacterium Synechocystis sp PCC 6803 and determined its crystal structure alone and in complex with various ligands. The protein consists of a core domain containing the catalytic site and a smaller cap domain that contains a glucose binding site. Two flexible hinge loops link the two domains, forming a structure that resembles a pair of sugar tongs. The glucose binding site plays a major role in determining the enzyme's remarkable substrate specificity and is also important for its inhibition by sucrose and glucose. It is proposed that the catalytic reaction is initiated by nucleophilic attack on the substrate by Asp9 and involves formation of a covalent phospho-Asp9-enzyme intermediate. From modeling based on the SPP structure, we predict that the noncatalytic SPP-like domain of the Synechocystis sucrose-phosphate synthase could bind sucrose-6(F)-phosphate and propose that this domain might be involved in metabolite channeling between the last two enzymes in the pathway of sucrose synthesis.

About this Structure

1S2O is a Single protein structure of sequence from Synechocystis sp.. Full crystallographic information is available from OCA.

Reference

The structure of a cyanobacterial sucrose-phosphatase reveals the sugar tongs that release free sucrose in the cell., Fieulaine S, Lunn JE, Borel F, Ferrer JL, Plant Cell. 2005 Jul;17(7):2049-58. Epub 2005 Jun 3. PMID:15937230

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