1iwl
From Proteopedia
(New page: 200px<br /><applet load="1iwl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iwl, resolution 1.65Å" /> '''Crystal Structure of...) |
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| - | [[Image:1iwl.gif|left|200px]]<br /><applet load="1iwl" size=" | + | [[Image:1iwl.gif|left|200px]]<br /><applet load="1iwl" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1iwl, resolution 1.65Å" /> | caption="1iwl, resolution 1.65Å" /> | ||
'''Crystal Structure of the Lipoprotein Localization Factor, LolA'''<br /> | '''Crystal Structure of the Lipoprotein Localization Factor, LolA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Lipoproteins having a lipid-modified cysteine at the N-terminus are | + | Lipoproteins having a lipid-modified cysteine at the N-terminus are localized on either the inner or the outer membrane of Escherichia coli depending on the residue at position 2. Five Lol proteins involved in the sorting and membrane localization of lipoprotein are highly conserved in Gram-negative bacteria. We determined the crystal structures of a periplasmic chaperone, LolA, and an outer membrane lipoprotein receptor, LolB. Despite their dissimilar amino acid sequences, the structures of LolA and LolB are strikingly similar to each other. Both have a hydrophobic cavity consisting of an unclosed beta barrel and an alpha-helical lid. The cavity represents a possible binding site for the lipid moiety of lipoproteins. Detailed structural differences between the two proteins provide significant insights into the molecular mechanisms underlying the energy-independent transfer of lipoproteins from LolA to LolB and from LolB to the outer membrane. Furthermore, the structures of both LolA and LolB determined from different crystal forms revealed the distinct structural dynamics regarding the association and dissociation of lipoproteins. The results are discussed in the context of the current model for the lipoprotein transfer from the inner to the outer membrane through a hydrophilic environment. |
==About this Structure== | ==About this Structure== | ||
| - | 1IWL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1IWL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IWL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: unclosed beta barrel]] | [[Category: unclosed beta barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:16:26 2008'' |
Revision as of 11:16, 21 February 2008
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Crystal Structure of the Lipoprotein Localization Factor, LolA
Overview
Lipoproteins having a lipid-modified cysteine at the N-terminus are localized on either the inner or the outer membrane of Escherichia coli depending on the residue at position 2. Five Lol proteins involved in the sorting and membrane localization of lipoprotein are highly conserved in Gram-negative bacteria. We determined the crystal structures of a periplasmic chaperone, LolA, and an outer membrane lipoprotein receptor, LolB. Despite their dissimilar amino acid sequences, the structures of LolA and LolB are strikingly similar to each other. Both have a hydrophobic cavity consisting of an unclosed beta barrel and an alpha-helical lid. The cavity represents a possible binding site for the lipid moiety of lipoproteins. Detailed structural differences between the two proteins provide significant insights into the molecular mechanisms underlying the energy-independent transfer of lipoproteins from LolA to LolB and from LolB to the outer membrane. Furthermore, the structures of both LolA and LolB determined from different crystal forms revealed the distinct structural dynamics regarding the association and dissociation of lipoproteins. The results are discussed in the context of the current model for the lipoprotein transfer from the inner to the outer membrane through a hydrophilic environment.
About this Structure
1IWL is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structures of bacterial lipoprotein localization factors, LolA and LolB., Takeda K, Miyatake H, Yokota N, Matsuyama S, Tokuda H, Miki K, EMBO J. 2003 Jul 1;22(13):3199-209. PMID:12839983
Page seeded by OCA on Thu Feb 21 13:16:26 2008
Categories: Escherichia coli | Single protein | Matsuyama, S. | Miki, K. | Miyatake, H. | Takeda, K. | Tokuda, H. | Yokota, N. | MG | ZN | Unclosed beta barrel
