4m56

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{{STRUCTURE_4m56| PDB=4m56 | SCENE= }}
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==The Structure of Wild-type MalL from Bacillus subtilis==
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===The Structure of Wild-type MalL from Bacillus subtilis===
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<StructureSection load='4m56' size='340' side='right' caption='[[4m56]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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{{ABSTRACT_PUBMED_24015933}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4m56]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M56 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M56 FirstGlance]. <br>
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==Function==
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLO:D-GLUCOSE+IN+LINEAR+FORM'>GLO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">malL, yvdL, BSU34560 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</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/Oligo-1,6-glucosidase Oligo-1,6-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.10 3.2.1.10] </span></td></tr>
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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=4m56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m56 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4m56 RCSB], [http://www.ebi.ac.uk/pdbsum/4m56 PDBsum]</span></td></tr>
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</table>
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== Function ==
[[http://www.uniprot.org/uniprot/O16G1_BACSU O16G1_BACSU]] Hydrolyzes various disaccharides such as sucrose, maltose, and isomaltose with different efficiencies. Also hydrolyzes longer maltodextrins from maltotriose up to maltohexaose, but not maltoheptaose, palatinose, isomaltotriose, or isomaltotetraose.
[[http://www.uniprot.org/uniprot/O16G1_BACSU O16G1_BACSU]] Hydrolyzes various disaccharides such as sucrose, maltose, and isomaltose with different efficiencies. Also hydrolyzes longer maltodextrins from maltotriose up to maltohexaose, but not maltoheptaose, palatinose, isomaltotriose, or isomaltotetraose.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The increase in enzymatic rates with temperature up to an optimum temperature (Topt) is widely attributed to classical Arrhenius behavior, with the decrease in enzymatic rates above Topt ascribed to protein denaturation and/or aggregation. This account persists despite many investigators noting that denaturation is insufficient to explain the decline in enzymatic rates above Topt. Here we show that it is the change in heat capacity associated with enzyme catalysis (DeltaCdouble daggerp) and its effect on the temperature dependence of DeltaGdouble dagger that determines the temperature dependence of enzyme activity. Through mutagenesis, we demonstrate that the Topt of an enzyme is correlated with DeltaCdouble daggerp and that changes to DeltaCdouble daggerp are sufficient to change Topt without affecting the catalytic rate. Furthermore, using X-ray crystallography and molecular dynamics simulations we reveal the molecular details underpinning these changes in DeltaCdouble daggerp. The influence of DeltaCdouble daggerp on enzymatic rates has implications for the temperature dependence of biological rates from enzymes to ecosystems.
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==About this Structure==
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Change in Heat Capacity for Enzyme Catalysis Determines Temperature Dependence of Enzyme Catalyzed Rates.,Hobbs JK, Jiao W, Easter AD, Parker EJ, Schipper LA, Arcus VL ACS Chem Biol. 2013 Sep 17. PMID:24015933<ref>PMID:24015933</ref>
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[[4m56]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M56 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:024015933</ref><references group="xtra"/><references/>
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</div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bacsu]]
[[Category: Bacsu]]
[[Category: Oligo-1,6-glucosidase]]
[[Category: Oligo-1,6-glucosidase]]
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[[Category: Arcus, V L.]]
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[[Category: Arcus, V L]]
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[[Category: Easter, A D.]]
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[[Category: Easter, A D]]
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[[Category: Hobbs, J K.]]
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[[Category: Hobbs, J K]]
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[[Category: Jiao, W.]]
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[[Category: Jiao, W]]
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[[Category: Parker, E J.]]
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[[Category: Parker, E J]]
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[[Category: Schipper, L A.]]
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[[Category: Schipper, L A]]
[[Category: Glucosidase]]
[[Category: Glucosidase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Tim barrel]]
[[Category: Tim barrel]]

Revision as of 06:03, 25 December 2014

The Structure of Wild-type MalL from Bacillus subtilis

4m56, resolution 2.30Å

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