1r7a: Difference between revisions

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<StructureSection load='1r7a' size='340' side='right'caption='[[1r7a]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
<StructureSection load='1r7a' size='340' side='right'caption='[[1r7a]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1r7a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/As_1.2190 As 1.2190]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R7A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R7A FirstGlance]. <br>
<table><tr><td colspan='2'>[[1r7a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bifidobacterium_adolescentis Bifidobacterium adolescentis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R7A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R7A FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.77&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Transferase Transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.7 2.4.1.7] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r7a OCA], [https://pdbe.org/1r7a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r7a RCSB], [https://www.ebi.ac.uk/pdbsum/1r7a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r7a ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r7a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r7a OCA], [https://pdbe.org/1r7a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r7a RCSB], [https://www.ebi.ac.uk/pdbsum/1r7a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r7a ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SUCP_BIFAA SUCP_BIFAA] Catalyzes the reversible phosphorolysis of sucrose into alpha-D-glucose 1-phosphate (Glc1P) and D-fructose (PubMed:14740189, PubMed:20691225). Is involved in sucrose degradation. Also displays transglucosylation activity in vitro, by transferring the glucosyl moiety of Glc1P to a broad range of monomeric sugars, such as D- and L-arabinose, D- and L-arabitol, and xylitol (PubMed:14740189).<ref>PMID:14740189</ref> <ref>PMID:20691225</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1r7a ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1r7a ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Around 80 enzymes are implicated in the generic starch and sucrose pathways. One of these enzymes is sucrose phosphorylase, which reversibly catalyzes the conversion of sucrose and orthophosphate to d-Fructose and alpha-d-glucose 1-phosphate. Here, we present the crystal structure of sucrose phosphorylase from Bifidobacterium adolescentis (BiSP) refined at 1.77 A resolution. It represents the first 3D structure of a sucrose phosphorylase and is the first structure of a phosphate-dependent enzyme from the glycoside hydrolase family 13. The structure of BiSP is composed of the four domains A, B, B', and C. Domain A comprises the (beta/alpha)(8)-barrel common to family 13. The catalytic active-site residues (Asp192 and Glu232) are located at the tips of beta-sheets 4 and 5 in the (beta/alpha)(8)-barrel, as required for family 13 members. The topology of the B' domain disfavors oligosaccharide binding and reduces the size of the substrate access channel compared to other family 13 members, underlining the role of this domain in modulating the function of these enzymes. It is remarkable that the fold of the C domain is not observed in any other known hydrolases of family 13. BiSP was found as a homodimer in the crystal, and a dimer contact surface area of 960 A(2) per monomer was calculated. The majority of the interactions are confined to the two B domains, but interactions between the loop 8 regions of the two barrels are also observed. This results in a large cavity in the dimer, including the entrance to the two active sites.
Crystal structure of sucrose phosphorylase from Bifidobacterium adolescentis.,Sprogoe D, van den Broek LA, Mirza O, Kastrup JS, Voragen AG, Gajhede M, Skov LK Biochemistry. 2004 Feb 10;43(5):1156-62. PMID:14756551<ref>PMID:14756551</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1r7a" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: As 1 2190]]
[[Category: Bifidobacterium adolescentis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Transferase]]
[[Category: Gajhede M]]
[[Category: Broek, L A.M van den]]
[[Category: Kastrup JS]]
[[Category: Gajhede, M]]
[[Category: Mirza O]]
[[Category: Kastrup, J S]]
[[Category: Skov LK]]
[[Category: Mirza, O]]
[[Category: Sprogoe D]]
[[Category: Skov, L K]]
[[Category: Voragen AGJ]]
[[Category: Sprogoe, D]]
[[Category: Van den Broek LAM]]
[[Category: Voragen, A G.J]]
[[Category: Beta-alpha-barrel]]
[[Category: Dimer]]
[[Category: Glycoside hydrolase]]

Revision as of 06:10, 17 April 2024

Sucrose Phosphorylase from Bifidobacterium adolescentis

1r7a, resolution 1.77Å

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