1rre: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
New page: left|200px<br /><applet load="1rre" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rre, resolution 1.75Å" /> '''Crystal structure of...
 
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1rre.jpg|left|200px]]<br /><applet load="1rre" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1rre.jpg|left|200px]]<br /><applet load="1rre" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1rre, resolution 1.75&Aring;" />
caption="1rre, resolution 1.75&Aring;" />
'''Crystal structure of E.coli Lon proteolytic domain'''<br />
'''Crystal structure of E.coli Lon proteolytic domain'''<br />


==Overview==
==Overview==
ATP-dependent Lon protease degrades specific short-lived regulatory, proteins as well as defective and abnormal proteins in the cell. The, crystal structure of the proteolytic domain (P domain) of the Escherichia, coli Lon has been solved by single-wavelength anomalous dispersion and, refined at 1.75-A resolution. The P domain was obtained by chymotrypsin, digestion of the full-length, proteolytically inactive Lon mutant (S679A), or by expression of a recombinant construct encoding only this domain. The, P domain has a unique fold and assembles into hexameric rings that likely, mimic the oligomerization state of the holoenzyme. The hexamer is, dome-shaped, with the six N termini oriented toward the narrower ring, surface, which is thus identified as the interface with the ATPase domain, in full-length Lon. The catalytic sites lie in a shallow concavity on the, wider distal surface of the hexameric ring and are connected to the, proximal surface by a narrow axial channel with a diameter of, approximately 18 A. Within the active site, the proximity of Lys(722) to, the side chain of the mutated Ala(679) and the absence of other potential, catalytic side chains establish that Lon employs a Ser(679)-Lys(722) dyad, for catalysis. Alignment of the P domain catalytic pocket with those of, several Ser-Lys dyad peptide hydrolases provides a model of substrate, binding, suggesting that polypeptides are oriented in the Lon active site, to allow nucleophilic attack by the serine hydroxyl on the si-face of the, peptide bond.
ATP-dependent Lon protease degrades specific short-lived regulatory proteins as well as defective and abnormal proteins in the cell. The crystal structure of the proteolytic domain (P domain) of the Escherichia coli Lon has been solved by single-wavelength anomalous dispersion and refined at 1.75-A resolution. The P domain was obtained by chymotrypsin digestion of the full-length, proteolytically inactive Lon mutant (S679A) or by expression of a recombinant construct encoding only this domain. The P domain has a unique fold and assembles into hexameric rings that likely mimic the oligomerization state of the holoenzyme. The hexamer is dome-shaped, with the six N termini oriented toward the narrower ring surface, which is thus identified as the interface with the ATPase domain in full-length Lon. The catalytic sites lie in a shallow concavity on the wider distal surface of the hexameric ring and are connected to the proximal surface by a narrow axial channel with a diameter of approximately 18 A. Within the active site, the proximity of Lys(722) to the side chain of the mutated Ala(679) and the absence of other potential catalytic side chains establish that Lon employs a Ser(679)-Lys(722) dyad for catalysis. Alignment of the P domain catalytic pocket with those of several Ser-Lys dyad peptide hydrolases provides a model of substrate binding, suggesting that polypeptides are oriented in the Lon active site to allow nucleophilic attack by the serine hydroxyl on the si-face of the peptide bond.


==About this Structure==
==About this Structure==
1RRE 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 SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RRE OCA].  
1RRE 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=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Endopeptidase_La Endopeptidase La], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.53 3.4.21.53] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RRE OCA].  


==Reference==
==Reference==
Line 18: Line 18:
[[Category: Dauter, Z.]]
[[Category: Dauter, Z.]]
[[Category: Gustchina, A.]]
[[Category: Gustchina, A.]]
[[Category: Khalatova, A.G.]]
[[Category: Khalatova, A G.]]
[[Category: Maurizi, M.R.]]
[[Category: Maurizi, M R.]]
[[Category: Melnikov, E.E.]]
[[Category: Melnikov, E E.]]
[[Category: Rasulova, F.]]
[[Category: Rasulova, F.]]
[[Category: Rotanova, T.V.]]
[[Category: Rotanova, T V.]]
[[Category: Tropea, J.E.]]
[[Category: Tropea, J E.]]
[[Category: Wlodawer, A.]]
[[Category: Wlodawer, A.]]
[[Category: SO4]]
[[Category: SO4]]
Line 29: Line 29:
[[Category: catalytic ser-lys dyad]]
[[Category: catalytic ser-lys dyad]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:49:08 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:53:47 2008''