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New page: left|200px<br /><applet load="1oul" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oul, resolution 2.20Å" /> '''Structure of the AAA...
 
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[[Image:1oul.jpg|left|200px]]<br /><applet load="1oul" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1oul.jpg|left|200px]]<br /><applet load="1oul" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1oul, resolution 2.20&Aring;" />
caption="1oul, resolution 2.20&Aring;" />
'''Structure of the AAA+ protease delivery protein SspB'''<br />
'''Structure of the AAA+ protease delivery protein SspB'''<br />


==Overview==
==Overview==
Substrate selection by AAA+ ATPases that function to unfold proteins or, alter protein conformation is often regulated by delivery or adaptor, proteins. SspB is a protein dimer that binds to the ssrA degradation tag, and delivers proteins bearing this tag to ClpXP, an AAA+ protease, for, degradation. Here, we describe the structure of the peptide binding domain, of H. influenzae SspB in complex with an ssrA peptide at 1.6 A resolution., The ssrA peptides are bound in well-defined clefts located at the extreme, ends of the SspB homodimer. SspB contacts residues within the N-terminal, and central regions of the 11 residue ssrA tag but leaves the C-terminal, residues exposed and positioned to dock with ClpX. This structure, taken, together with biochemical analysis of SspB, suggests mechanisms by which, proteins like SspB escort substrates to AAA+ ATPases and enhance the, specificity and affinity of target recognition.
Substrate selection by AAA+ ATPases that function to unfold proteins or alter protein conformation is often regulated by delivery or adaptor proteins. SspB is a protein dimer that binds to the ssrA degradation tag and delivers proteins bearing this tag to ClpXP, an AAA+ protease, for degradation. Here, we describe the structure of the peptide binding domain of H. influenzae SspB in complex with an ssrA peptide at 1.6 A resolution. The ssrA peptides are bound in well-defined clefts located at the extreme ends of the SspB homodimer. SspB contacts residues within the N-terminal and central regions of the 11 residue ssrA tag but leaves the C-terminal residues exposed and positioned to dock with ClpX. This structure, taken together with biochemical analysis of SspB, suggests mechanisms by which proteins like SspB escort substrates to AAA+ ATPases and enhance the specificity and affinity of target recognition.


==About this Structure==
==About this Structure==
1OUL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OUL OCA].  
1OUL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OUL OCA].  


==Reference==
==Reference==
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[[Category: Haemophilus influenzae]]
[[Category: Haemophilus influenzae]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Baker, T.A.]]
[[Category: Baker, T A.]]
[[Category: Grant, R.A.]]
[[Category: Grant, R A.]]
[[Category: Levchenko, I.]]
[[Category: Levchenko, I.]]
[[Category: Sauer, R.T.]]
[[Category: Sauer, R T.]]
[[Category: Wah, D.A.]]
[[Category: Wah, D A.]]
[[Category: homodimer]]
[[Category: homodimer]]
[[Category: ssra peptide binding protein]]
[[Category: ssra peptide binding protein]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:12:44 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:49 2008''