1xgz

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{{Seed}}
 
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[[Image:1xgz.png|left|200px]]
 
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==Structure of the N298S variant of human pancreatic alpha-amylase==
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The line below this paragraph, containing "STRUCTURE_1xgz", creates the "Structure Box" on the page.
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<StructureSection load='1xgz' size='340' side='right'caption='[[1xgz]], [[Resolution|resolution]] 2.00&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'>[[1xgz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XGZ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
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{{STRUCTURE_1xgz| PDB=1xgz | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xgz OCA], [https://pdbe.org/1xgz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xgz RCSB], [https://www.ebi.ac.uk/pdbsum/1xgz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xgz ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AMYP_HUMAN AMYP_HUMAN]
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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/xg/1xgz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1xgz 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 mechanism of allosteric activation of alpha-amylase by chloride has been studied through structural and kinetic experiments focusing on the chloride-dependent N298S variant of human pancreatic alpha-amylase (HPA) and a chloride-independent TAKA-amylase. Kinetic analysis of the HPA variant clearly demonstrates the pronounced activating effect of chloride ion binding on reaction rates and its effect on the pH-dependence of catalysis. Structural alterations observed in the N298S variant upon chloride ion binding suggest that the chloride ion plays a variety of roles that serve to promote catalysis. One of these is having a strong influence on the positioning of the acid/base catalyst residue E233. Absence of chloride ion results in multiple conformations for this residue and unexpected enzymatic products. Chloride ion and N298 also appear to stabilize a helical region of polypeptide chain from which projects the flexible substrate binding loop unique to chloride-dependent alpha-amylases. This structural feature also serves to properly orient the catalytically essential residue D300. Comparative analyses show that the chloride-independent alpha-amylases compensate for the absence of bound chloride by substituting a hydrophobic core, altering the manner in which substrate interactions are made and shifting the placement of N298. These evolutionary differences presumably arise in response to alternative operating environments or the advantage gained in a particular product profile. Attempts to engineer chloride-dependence into the chloride-independent TAKA-amylase point out the complexity of this system, and the fact that a multitude of factors play a role in binding chloride ion in the chloride-dependent alpha-amylases.
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===Structure of the N298S variant of human pancreatic alpha-amylase===
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Structural and mechanistic studies of chloride induced activation of human pancreatic alpha-amylase.,Maurus R, Begum A, Kuo HH, Racaza A, Numao S, Andersen C, Tams JW, Vind J, Overall CM, Withers SG, Brayer GD Protein Sci. 2005 Mar;14(3):743-55. PMID:15722449<ref>PMID:15722449</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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<div class="pdbe-citations 1xgz" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15722449}}, adds the Publication Abstract to the page
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*[[Amylase 3D structures|Amylase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15722449 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15722449}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1XGZ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XGZ OCA].
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==Reference==
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<ref group="xtra">PMID:15722449</ref><references group="xtra"/>
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[[Category: Alpha-amylase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Begum, A.]]
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[[Category: Large Structures]]
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[[Category: Brayer, G D.]]
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[[Category: Begum A]]
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[[Category: Kuo, H H.]]
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[[Category: Brayer GD]]
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[[Category: Maurus, R.]]
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[[Category: Kuo HH]]
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[[Category: Numao, S.]]
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[[Category: Maurus R]]
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[[Category: Overall, C M.]]
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[[Category: Numao S]]
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[[Category: Racaza, A.]]
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[[Category: Overall CM]]
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[[Category: Withers, S G.]]
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[[Category: Racaza A]]
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[[Category: Acarbose]]
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[[Category: Withers SG]]
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[[Category: Amylase]]
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[[Category: Chloride]]
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[[Category: Enzyme]]
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[[Category: Inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 13:46:27 2009''
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Current revision

Structure of the N298S variant of human pancreatic alpha-amylase

PDB ID 1xgz

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