1qwd
From Proteopedia
(New page: 200px<br /><applet load="1qwd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qwd, resolution 1.75Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1qwd.gif|left|200px]]<br /><applet load="1qwd" size=" | + | [[Image:1qwd.gif|left|200px]]<br /><applet load="1qwd" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qwd, resolution 1.75Å" /> | caption="1qwd, resolution 1.75Å" /> | ||
'''CRYSTAL STRUCTURE OF A BACTERIAL LIPOCALIN, THE BLC GENE PRODUCT FROM E. COLI'''<br /> | '''CRYSTAL STRUCTURE OF A BACTERIAL LIPOCALIN, THE BLC GENE PRODUCT FROM E. COLI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Lipocalins form a large multifunctional family of small proteins (15-25 | + | Lipocalins form a large multifunctional family of small proteins (15-25 kDa) first discovered in eukaryotes. More recently, several types of bacterial lipocalins have been reported, among which Blc from Escherichia coli is an outer membrane lipoprotein. As part of our structural genomics effort on proteins from E. coli, we have expressed, crystallized and solved the structure of Blc at 1.8 A resolution using remote SAD with xenon. The structure of Blc, the first of a bacterial lipocalin, exhibits a classical fold formed by a beta-barrel and a alpha-helix similar to that of the moth bilin binding protein. Its empty and open cavity, however, is too narrow to accommodate bilin, while the alkyl chains of two fatty acids or of a phospholipid could be readily modeled inside the cavity. Blc was reported to be expressed under stress conditions such as starvation or high osmolarity, during which the cell envelope suffers and requires maintenance. These data, together with our structural interpretation, suggest a role for Blc in storage or transport of lipids necessary for membrane repair or maintenance. |
==About this Structure== | ==About this Structure== | ||
| - | 1QWD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1QWD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: bacterial lipocalin]] | [[Category: bacterial lipocalin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:44:30 2008'' |
Revision as of 12:44, 21 February 2008
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CRYSTAL STRUCTURE OF A BACTERIAL LIPOCALIN, THE BLC GENE PRODUCT FROM E. COLI
Overview
Lipocalins form a large multifunctional family of small proteins (15-25 kDa) first discovered in eukaryotes. More recently, several types of bacterial lipocalins have been reported, among which Blc from Escherichia coli is an outer membrane lipoprotein. As part of our structural genomics effort on proteins from E. coli, we have expressed, crystallized and solved the structure of Blc at 1.8 A resolution using remote SAD with xenon. The structure of Blc, the first of a bacterial lipocalin, exhibits a classical fold formed by a beta-barrel and a alpha-helix similar to that of the moth bilin binding protein. Its empty and open cavity, however, is too narrow to accommodate bilin, while the alkyl chains of two fatty acids or of a phospholipid could be readily modeled inside the cavity. Blc was reported to be expressed under stress conditions such as starvation or high osmolarity, during which the cell envelope suffers and requires maintenance. These data, together with our structural interpretation, suggest a role for Blc in storage or transport of lipids necessary for membrane repair or maintenance.
About this Structure
1QWD is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The crystal structure of the Escherichia coli lipocalin Blc suggests a possible role in phospholipid binding., Campanacci V, Nurizzo D, Spinelli S, Valencia C, Tegoni M, Cambillau C, FEBS Lett. 2004 Mar 26;562(1-3):183-8. PMID:15044022
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