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PDBsum entry 1jjw
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure of haemophilus influenzae hslv protein at 1.9 a resolution, Revealing a cation-Binding site near the catalytic site.
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Authors
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M.C.Sousa,
D.B.Mckay.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2001,
57,
1950-1954.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 1.
Figure 1 Quasi-equivalent subunit interactions within HslV. (a)
Ribbon drawing of one hexamer, looking down the pseudo-sixfold
axis. Subunits related by crystallographic twofold rotation are
shown in identical colors and denoted with a prime. Regions on
the apical helices which reveal differences in subunit-subunit
interactions are highlighted: magenta on cyan for subunit A; red
on yellow for subunit B; green on gold for subunit C. (b)
Interactions between subunits C and A, using same color coding
as in (a). (c) Interactions between subunits B and C. Figs.
1-and 2-(b) were produced with MOLSCRIPT (Kraulis, 1991[Kraulis,
P. (1991). J. Appl. Cryst. 24, 946-950.]) and Fig. 2-(a) was
produced with BOBSCRIPT (Esnouf, 1997[Esnouf, R. M. (1997). J.
Mol. Graph. 15, 132-134.], 1999[Esnouf, R. M. (1999). Acta
Cryst. D55, 938-940.]); all figures were rendered with Raster3D
(Merritt & Bacon, 1997[Merritt, E. A. & Bacon, D. J. (1997).
Methods Enzymol. 277, 505-524.]).
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The above figure is
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2001,
57,
1950-1954)
copyright 2001.
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