1jjw
From Proteopedia
(New page: 200px<br /><applet load="1jjw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jjw, resolution 1.90Å" /> '''Structure of Haemoph...) |
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| - | [[Image:1jjw.gif|left|200px]]<br /><applet load="1jjw" size=" | + | [[Image:1jjw.gif|left|200px]]<br /><applet load="1jjw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jjw, resolution 1.90Å" /> | caption="1jjw, resolution 1.90Å" /> | ||
'''Structure of Haemophilus influenzae HslV Protein at 1.9 A Resolution'''<br /> | '''Structure of Haemophilus influenzae HslV Protein at 1.9 A Resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the Haemophilus influenzae HslV protease of the HslUV | + | The structure of the Haemophilus influenzae HslV protease of the HslUV 'prokaryotic proteasome' has been solved by molecular replacement and refined with data to 1.9 A resolution. The protease is a 'double donut' of hexameric rings; two alternative sets of intermolecular interactions between protomers in the rings result in 'quasi-equivalent' packing within the assembly. Anomalous scattering data from crystals with potassium present in the mother liquor reveal a K(+) ion bound with octahedral coordination near the active-site Thr1 residue. The site also binds Na(+) ions and is likely to bind Mg(2+), suggesting that monovalent and divalent metal ions may influence the catalytic activity of the protease. |
==About this Structure== | ==About this Structure== | ||
| - | 1JJW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with K as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1JJW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with <scene name='pdbligand=K:'>K</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JJW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Haemophilus influenzae]] | [[Category: Haemophilus influenzae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: McKay, D | + | [[Category: McKay, D B.]] |
| - | [[Category: Sousa, M | + | [[Category: Sousa, M C.]] |
[[Category: K]] | [[Category: K]] | ||
[[Category: k anomalous scattering]] | [[Category: k anomalous scattering]] | ||
[[Category: quasi-equivalent packing]] | [[Category: quasi-equivalent packing]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:23:30 2008'' |
Revision as of 11:23, 21 February 2008
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Structure of Haemophilus influenzae HslV Protein at 1.9 A Resolution
Overview
The structure of the Haemophilus influenzae HslV protease of the HslUV 'prokaryotic proteasome' has been solved by molecular replacement and refined with data to 1.9 A resolution. The protease is a 'double donut' of hexameric rings; two alternative sets of intermolecular interactions between protomers in the rings result in 'quasi-equivalent' packing within the assembly. Anomalous scattering data from crystals with potassium present in the mother liquor reveal a K(+) ion bound with octahedral coordination near the active-site Thr1 residue. The site also binds Na(+) ions and is likely to bind Mg(2+), suggesting that monovalent and divalent metal ions may influence the catalytic activity of the protease.
About this Structure
1JJW is a Single protein structure of sequence from Haemophilus influenzae with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of Haemophilus influenzae HslV protein at 1.9 A resolution, revealing a cation-binding site near the catalytic site., Sousa MC, McKay DB, Acta Crystallogr D Biol Crystallogr. 2001 Dec;57(Pt 12):1950-4. Epub 2001, Nov 21. PMID:11717526
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