2enx: Difference between revisions

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==Overview==

Streptococcus agalactiae, a prokaryote that causes infections in neonates, and immunocompromised adults, has a serine/threonine protein kinase (STK), signalling cascade. The structure of one of the targets, a family II, inorganic pyrophosphatase, has been solved by molecular replacement and, refined at 2.80 A resolution to an R factor of 19.2% (R(free) = 26.7%)., The two monomers in the asymmetric unit are related by a, noncrystallographic twofold axis, but the biological dimer is formed by a, crystallographic twofold. Each monomer contains the pyrophosphate analogue, imidodiphosphate (PNP) and three metal ions per active site: two Mn(2+), ions in sites M1 and M2 and an Mg(2+) ion in site M3. The enzyme is in the, closed conformation. Like other family II enzymes, the structure consists, of two domains (residues 1-191 and 198-311), with the active site located, between them. The conformation of Lys298 in the active site is different, from those observed previously and it coordinates to the conserved DHH, motif in a unique way. The structure suggests that Ser150, Ser194, Ser195, and Ser296 are the most likely targets for the Ser/Thr kinase and, phosphatase because they are surface-accessible and either in the active, site or in the hinge region between the two domains.

Streptococcus agalactiae, a prokaryote that causes infections in neonates and immunocompromised adults, has a serine/threonine protein kinase (STK) signalling cascade. The structure of one of the targets, a family II inorganic pyrophosphatase, has been solved by molecular replacement and refined at 2.80 A resolution to an R factor of 19.2% (R(free) = 26.7%). The two monomers in the asymmetric unit are related by a noncrystallographic twofold axis, but the biological dimer is formed by a crystallographic twofold. Each monomer contains the pyrophosphate analogue imidodiphosphate (PNP) and three metal ions per active site: two Mn(2+) ions in sites M1 and M2 and an Mg(2+) ion in site M3. The enzyme is in the closed conformation. Like other family II enzymes, the structure consists of two domains (residues 1-191 and 198-311), with the active site located between them. The conformation of Lys298 in the active site is different from those observed previously and it coordinates to the conserved DHH motif in a unique way. The structure suggests that Ser150, Ser194, Ser195 and Ser296 are the most likely targets for the Ser/Thr kinase and phosphatase because they are surface-accessible and either in the active site or in the hinge region between the two domains.

==About this Structure==

Line 17:

[[Category: Lehtio, L.]]

[[Category: Rajagopal, L.]]

[[Category: Rantanen, M.K.]]

[[Category: Rantanen, M K.]]

[[Category: Rubens, C.E.]]

[[Category: Rubens, C E.]]

[[Category: 2PN]]

[[Category: MG]]

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[[Category: streptococcus agalactiae]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-Streptococcus agalactiae, a prokaryote that causes infections in neonates, and immunocompromised adults, has a serine/threonine protein kinase (STK), signalling cascade. The structure of one of the targets, a family II, inorganic pyrophosphatase, has been solved by molecular replacement and, refined at 2.80 A resolution to an R factor of 19.2% (R(free) = 26.7%)., The two monomers in the asymmetric unit are related by a, noncrystallographic twofold axis, but the biological dimer is formed by a, crystallographic twofold. Each monomer contains the pyrophosphate analogue, imidodiphosphate (PNP) and three metal ions per active site: two Mn(2+), ions in sites M1 and M2 and an Mg(2+) ion in site M3. The enzyme is in the, closed conformation. Like other family II enzymes, the structure consists, of two domains (residues 1-191 and 198-311), with the active site located, between them. The conformation of Lys298 in the active site is different, from those observed previously and it coordinates to the conserved DHH, motif in a unique way. The structure suggests that Ser150, Ser194, Ser195, and Ser296 are the most likely targets for the Ser/Thr kinase and, phosphatase because they are surface-accessible and either in the active, site or in the hinge region between the two domains.
+Streptococcus agalactiae, a prokaryote that causes infections in neonates and immunocompromised adults, has a serine/threonine protein kinase (STK) signalling cascade. The structure of one of the targets, a family II inorganic pyrophosphatase, has been solved by molecular replacement and refined at 2.80 A resolution to an R factor of 19.2% (R(free) = 26.7%). The two monomers in the asymmetric unit are related by a noncrystallographic twofold axis, but the biological dimer is formed by a crystallographic twofold. Each monomer contains the pyrophosphate analogue imidodiphosphate (PNP) and three metal ions per active site: two Mn(2+) ions in sites M1 and M2 and an Mg(2+) ion in site M3. The enzyme is in the closed conformation. Like other family II enzymes, the structure consists of two domains (residues 1-191 and 198-311), with the active site located between them. The conformation of Lys298 in the active site is different from those observed previously and it coordinates to the conserved DHH motif in a unique way. The structure suggests that Ser150, Ser194, Ser195 and Ser296 are the most likely targets for the Ser/Thr kinase and phosphatase because they are surface-accessible and either in the active site or in the hinge region between the two domains.
 ==About this Structure==
@@ Line 17: / Line 17: @@
 [[Category: Lehtio, L.]]
 [[Category: Rajagopal, L.]]
-[[Category: Rantanen, M.K.]]
+[[Category: Rantanen, M K.]]
-[[Category: Rubens, C.E.]]
+[[Category: Rubens, C E.]]
 [[Category: 2PN]]
 [[Category: MG]]
@@ Line 30: / Line 30: @@
 [[Category: streptococcus agalactiae]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:52:36 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:12:57 2008''