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9gpb

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{{Seed}}
 
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[[Image:9gpb.png|left|200px]]
 
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==THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE==
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The line below this paragraph, containing "STRUCTURE_9gpb", creates the "Structure Box" on the page.
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<StructureSection load='9gpb' size='340' side='right' caption='[[9gpb]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[9gpb]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9GPB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=9GPB FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </span></td></tr>
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{{STRUCTURE_9gpb| PDB=9gpb | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=9gpb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9gpb OCA], [http://pdbe.org/9gpb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=9gpb RCSB], [http://www.ebi.ac.uk/pdbsum/9gpb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=9gpb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/PYGM_RABIT PYGM_RABIT]] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gp/9gpb_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=9gpb ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The crystal structure of R-state glycogen phosphorylase b has been determined at 2.9 A resolution. A comparison of T-state and R-state structures of the enzyme explains its cooperative behaviour on ligand binding and the allosteric regulation of its activity. Communication between catalytic sites of the dimer is provided by a change in packing geometry of two helices linking each site with the subunit interface. Activation by AMP or by phosphorylation results in a quaternary conformational change that switches these two helices into the R-state conformation.
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===THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE===
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The allosteric transition of glycogen phosphorylase.,Barford D, Johnson LN Nature. 1989 Aug 24;340(6235):609-16. PMID:2770867<ref>PMID:2770867</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_2770867}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 9gpb" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 2770867 is the PubMed ID number.
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== References ==
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-->
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<references/>
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{{ABSTRACT_PUBMED_2770867}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: European rabbit]]
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9GPB is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9GPB OCA].
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==Reference==
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<ref group="xtra">PMID:2770867</ref><references group="xtra"/>
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[[Category: Oryctolagus cuniculus]]
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[[Category: Phosphorylase]]
[[Category: Phosphorylase]]
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[[Category: Barford, D.]]
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[[Category: Barford, D]]
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[[Category: Johnson, L N.]]
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[[Category: Johnson, L N]]
[[Category: Glycogen phosphorylase]]
[[Category: Glycogen phosphorylase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 13:43:31 2009''
 

Current revision

THE ALLOSTERIC TRANSITION OF GLYCOGEN PHOSPHORYLASE

9gpb, resolution 2.90Å

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