1ku0: Difference between revisions
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New page: left|200px<br /><applet load="1ku0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ku0, resolution 2.0Å" /> '''Structure of the Baci... |
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[[Image:1ku0.jpg|left|200px]]<br /><applet load="1ku0" size=" | [[Image:1ku0.jpg|left|200px]]<br /><applet load="1ku0" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ku0, resolution 2.0Å" /> | caption="1ku0, resolution 2.0Å" /> | ||
'''Structure of the Bacillus stearothermophilus L1 lipase'''<br /> | '''Structure of the Bacillus stearothermophilus L1 lipase'''<br /> | ||
==Overview== | ==Overview== | ||
The bacterial thermoalkalophilic lipases optimally hydrolyze saturated | The bacterial thermoalkalophilic lipases optimally hydrolyze saturated fatty acids at elevated temperatures. They also have significant sequence homology with staphylococcal lipases, and both the thermoalkalophilic and staphylococcal lipases are grouped as the lipase family I.5. We report here the first crystal structure of the lipase family I.5, the structure of a thermoalkalophilic lipase from Bacillus stearothermophilus L1 (L1 lipase) determined at 2.0-A resolution. The structure is in a closed conformation, and the active site is buried under a long lid helix. Unexpectedly, the structure exhibits a zinc-binding site in an extra domain that accounts for the larger molecular size of the family I.5 enzymes in comparison to other microbial lipases. The zinc-coordinated extra domain makes tight interactions with the loop extended from the C terminus of the lid helix, suggesting that the activation of the family I.5 lipases may be regulated by the strength of the interactions. The unusually long lid helix makes strong hydrophobic interactions with its neighbors. The structural information together with previous biochemical observations indicate that the temperature-mediated lid opening is triggered by the thermal dissociation of the hydrophobic interactions. | ||
==About this Structure== | ==About this Structure== | ||
1KU0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with ZN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] Full crystallographic information is available from [http:// | 1KU0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KU0 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Triacylglycerol lipase]] | [[Category: Triacylglycerol lipase]] | ||
[[Category: Chi, S | [[Category: Chi, S W.]] | ||
[[Category: Jeong, S | [[Category: Jeong, S T.]] | ||
[[Category: Kim, H | [[Category: Kim, H K.]] | ||
[[Category: Kim, S | [[Category: Kim, S J.]] | ||
[[Category: Oh, T | [[Category: Oh, T K.]] | ||
[[Category: Pan, J | [[Category: Pan, J G.]] | ||
[[Category: Ryu, S | [[Category: Ryu, S E.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: lipase]] | [[Category: lipase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:37:56 2008'' | ||