1iwl
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1iwl |SIZE=350|CAPTION= <scene name='initialview01'>1iwl</scene>, resolution 1.65Å | |PDB= 1iwl |SIZE=350|CAPTION= <scene name='initialview01'>1iwl</scene>, resolution 1.65Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1iwm|1IWM]], [[1iwn|1IWN]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iwl OCA], [http://www.ebi.ac.uk/pdbsum/1iwl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1iwl RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Tokuda, H.]] | [[Category: Tokuda, H.]] | ||
[[Category: Yokota, N.]] | [[Category: Yokota, N.]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: ZN]] | ||
[[Category: unclosed beta barrel]] | [[Category: unclosed beta barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:25:39 2008'' |
Revision as of 18:25, 30 March 2008
| |||||||
| , resolution 1.65Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1IWM, 1IWN
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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