3blc
From Proteopedia
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| - | [[Image:3blc.jpg|left|200px]] | + | [[Image:3blc.jpg|left|200px]] |
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| - | '''Crystal structure of the periplasmic domain of the Escherichia Coli YIDC''' | + | {{Structure |
| + | |PDB= 3blc |SIZE=350|CAPTION= <scene name='initialview01'>3blc</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= oxaA, yidC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the periplasmic domain of the Escherichia Coli YIDC''' | ||
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| + | ==Overview== | ||
| + | The essential bacterial membrane protein YidC facilitates insertion and assembly of proteins destined for integration into the inner membrane. It has homologues in both mitochondria and chloroplasts. Here we report the crystal structure of the Escherichia coli YidC major periplasmic domain (YidCECP1) at 2.5A resolution. This domain is present in YidC from Gram-negative bacteria and is more than half the size of the full-length protein. The structure reveals that YidCECP1 is made up of a large twisted beta-sandwich protein fold with a C-terminal alpha-helix that packs against one face of the beta-sandwich. Our structure and sequence analysis reveals that the C-terminal alpha-helix and the beta-sheet that it lays against are the most conserved regions of the domain. The region corresponding to the C-terminal alpha-helix was previously shown to be important for the protein insertase function of YidC and is conserved in other YidC-like proteins. The structure reveals that a region of YidC that was previously shown to be involved in binding to SecF maps to one edge of the beta-sandwich. Electrostatic analysis of the molecular surface for this region of YidC reveals a predominantly charged surface and suggests that the SecF-YidC interaction may be electrostatic in nature. Interestingly, YidCECP1 has significant structural similarity to galactose mutarotase from Lactococcus lactis, suggesting that this domain may have another function besides its role in membrane protein assembly. | ||
==About this Structure== | ==About this Structure== | ||
| - | 3BLC is a [ | + | 3BLC is a [[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=3BLC OCA]. |
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| + | ==Reference== | ||
| + | Crystal structure of the major periplasmic domain of the bacterial membrane protein assembly facilitator YidC., Oliver DC, Paetzel M, J Biol Chem. 2008 Feb 22;283(8):5208-16. Epub 2007 Dec 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18093969 18093969] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Paetzel, M.]] | [[Category: Paetzel, M.]] | ||
[[Category: chaperone]] | [[Category: chaperone]] | ||
| + | [[Category: chaperone,protein transport]] | ||
[[Category: inner membrane]] | [[Category: inner membrane]] | ||
[[Category: membrane assembly facilitator]] | [[Category: membrane assembly facilitator]] | ||
[[Category: oxaa]] | [[Category: oxaa]] | ||
[[Category: periplasmic domain]] | [[Category: periplasmic domain]] | ||
| - | [[Category: protein transport]] | ||
[[Category: transmembrane]] | [[Category: transmembrane]] | ||
[[Category: yidc]] | [[Category: yidc]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:59:54 2008'' |
Revision as of 16:59, 20 March 2008
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| , resolution 2.50Å | |||||||
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| Gene: | oxaA, yidC (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the periplasmic domain of the Escherichia Coli YIDC
Overview
The essential bacterial membrane protein YidC facilitates insertion and assembly of proteins destined for integration into the inner membrane. It has homologues in both mitochondria and chloroplasts. Here we report the crystal structure of the Escherichia coli YidC major periplasmic domain (YidCECP1) at 2.5A resolution. This domain is present in YidC from Gram-negative bacteria and is more than half the size of the full-length protein. The structure reveals that YidCECP1 is made up of a large twisted beta-sandwich protein fold with a C-terminal alpha-helix that packs against one face of the beta-sandwich. Our structure and sequence analysis reveals that the C-terminal alpha-helix and the beta-sheet that it lays against are the most conserved regions of the domain. The region corresponding to the C-terminal alpha-helix was previously shown to be important for the protein insertase function of YidC and is conserved in other YidC-like proteins. The structure reveals that a region of YidC that was previously shown to be involved in binding to SecF maps to one edge of the beta-sandwich. Electrostatic analysis of the molecular surface for this region of YidC reveals a predominantly charged surface and suggests that the SecF-YidC interaction may be electrostatic in nature. Interestingly, YidCECP1 has significant structural similarity to galactose mutarotase from Lactococcus lactis, suggesting that this domain may have another function besides its role in membrane protein assembly.
About this Structure
3BLC is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of the major periplasmic domain of the bacterial membrane protein assembly facilitator YidC., Oliver DC, Paetzel M, J Biol Chem. 2008 Feb 22;283(8):5208-16. Epub 2007 Dec 19. PMID:18093969
Page seeded by OCA on Thu Mar 20 18:59:54 2008
