1ozb
From Proteopedia
(New page: 200px<br /><applet load="1ozb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ozb, resolution 2.80Å" /> '''Crystal Structure of...) |
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| - | [[Image:1ozb.gif|left|200px]]<br /><applet load="1ozb" size=" | + | [[Image:1ozb.gif|left|200px]]<br /><applet load="1ozb" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ozb, resolution 2.80Å" /> | caption="1ozb, resolution 2.80Å" /> | ||
'''Crystal Structure of SecB complexed with SecA C-terminus'''<br /> | '''Crystal Structure of SecB complexed with SecA C-terminus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | SecB is a bacterial chaperone involved in directing pre-protein to the | + | SecB is a bacterial chaperone involved in directing pre-protein to the translocation pathway by its specific interaction with the peripheral membrane ATPase SecA. The SecB-binding site on SecA is located at its C terminus and consists of a stretch of highly conserved residues. The crystal structure of SecB in complex with the C-terminal 27 amino acids of SecA from Haemophilus influenzae shows that the SecA peptide is structured as a CCCH zinc-binding motif. One SecB tetramer is bound by two SecA peptides, and the interface involves primarily salt bridges and hydrogen bonding interactions. The structure explains the importance of the zinc-binding motif and conserved residues at the C terminus of SecA in its high-affinity binding with SecB. It also suggests a model of SecB-SecA interaction and its implication for the mechanism of pre-protein transfer in bacterial protein translocation. |
==About this Structure== | ==About this Structure== | ||
| - | 1OZB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1OZB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OZB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zinc binding motif]] | [[Category: zinc binding motif]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:23:20 2008'' |
Revision as of 12:23, 21 February 2008
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Crystal Structure of SecB complexed with SecA C-terminus
Overview
SecB is a bacterial chaperone involved in directing pre-protein to the translocation pathway by its specific interaction with the peripheral membrane ATPase SecA. The SecB-binding site on SecA is located at its C terminus and consists of a stretch of highly conserved residues. The crystal structure of SecB in complex with the C-terminal 27 amino acids of SecA from Haemophilus influenzae shows that the SecA peptide is structured as a CCCH zinc-binding motif. One SecB tetramer is bound by two SecA peptides, and the interface involves primarily salt bridges and hydrogen bonding interactions. The structure explains the importance of the zinc-binding motif and conserved residues at the C terminus of SecA in its high-affinity binding with SecB. It also suggests a model of SecB-SecA interaction and its implication for the mechanism of pre-protein transfer in bacterial protein translocation.
About this Structure
1OZB is a Protein complex structure of sequences from Haemophilus influenzae with as ligand. Full crystallographic information is available from OCA.
Reference
Structural determinants of SecB recognition by SecA in bacterial protein translocation., Zhou J, Xu Z, Nat Struct Biol. 2003 Nov;10(11):942-7. Epub 2003 Sep 28. PMID:14517549
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