1j8d: Difference between revisions

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[[Image:1j8d.jpg|left|200px]]<br /><applet load="1j8d" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1j8d.jpg|left|200px]]<br /><applet load="1j8d" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1j8d, resolution 2.3Å" />

'''Structure Of the metal-free form of the deoxy-D-mannose-octulosonate 8-phosphate phosphatase (YrbI) From Haemophilus Influenzae (HI1679)'''<br />

==Overview==

The crystal structure of the YrbI protein from Haemophilus influenzae, (HI1679) was determined at a 1.67-A resolution. The function of the, protein had not been assigned previously, and it is annotated as, hypothetical in sequence databases. The protein exhibits the, alpha/beta-hydrolase fold (also termed the Rossmann fold) and resembles, most closely the fold of the L-2-haloacid dehalogenase (HAD) superfamily., Following this observation, a detailed sequence analysis revealed remote, homology to two members of the HAD superfamily, the P-domain of Ca(2+), ATPase and phosphoserine phosphatase. The 19-kDa chains of HI1679 form a, tetramer both in solution and in the crystalline form. The four monomers, are arranged in a ring such that four beta-hairpin loops, each inserted, after the first beta-strand of the core alpha/beta-fold, form an, eight-stranded barrel at the center of the assembly. Four active sites are, located at the subunit interfaces. Each active site is occupied by a, cobalt ion, a metal used for crystallization. The cobalt is octahedrally, coordinated to two aspartate side-chains, a backbone oxygen, and three, solvent molecules, indicating that the physiological metal may be, magnesium. HI1679 hydrolyzes a number of phosphates, including, 6-phosphogluconate and phosphotyrosine, suggesting that it functions as a, phosphatase in vivo. The physiological substrate is yet to be identified;, however the location of the gene on the yrb operon suggests involvement in, sugar metabolism.

The crystal structure of the YrbI protein from Haemophilus influenzae (HI1679) was determined at a 1.67-A resolution. The function of the protein had not been assigned previously, and it is annotated as hypothetical in sequence databases. The protein exhibits the alpha/beta-hydrolase fold (also termed the Rossmann fold) and resembles most closely the fold of the L-2-haloacid dehalogenase (HAD) superfamily. Following this observation, a detailed sequence analysis revealed remote homology to two members of the HAD superfamily, the P-domain of Ca(2+) ATPase and phosphoserine phosphatase. The 19-kDa chains of HI1679 form a tetramer both in solution and in the crystalline form. The four monomers are arranged in a ring such that four beta-hairpin loops, each inserted after the first beta-strand of the core alpha/beta-fold, form an eight-stranded barrel at the center of the assembly. Four active sites are located at the subunit interfaces. Each active site is occupied by a cobalt ion, a metal used for crystallization. The cobalt is octahedrally coordinated to two aspartate side-chains, a backbone oxygen, and three solvent molecules, indicating that the physiological metal may be magnesium. HI1679 hydrolyzes a number of phosphates, including 6-phosphogluconate and phosphotyrosine, suggesting that it functions as a phosphatase in vivo. The physiological substrate is yet to be identified; however the location of the gene on the yrb operon suggests involvement in sugar metabolism.

==About this Structure==

1J8D 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 GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1J8D OCA].

1J8D 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=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J8D OCA].

==Reference==

Line 15:

[[Category: Herzberg, O.]]

[[Category: Lim, K.]]

[[Category: S2F, Structure.2.Function.Project.]]

[[Category: S2F, Structure 2.Function Project.]]

[[Category: GOL]]

[[Category: hi1679]]

Line 23:

[[Category: structure 2 function project]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:19:52 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1j8d.jpg|left|200px]]<br /><applet load="1j8d" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1j8d.jpg|left|200px]]<br /><applet load="1j8d" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1j8d, resolution 2.3&Aring;" />
 '''Structure Of the metal-free form of the deoxy-D-mannose-octulosonate 8-phosphate phosphatase (YrbI) From Haemophilus Influenzae (HI1679)'''<br />
 ==Overview==
-The crystal structure of the YrbI protein from Haemophilus influenzae, (HI1679) was determined at a 1.67-A resolution. The function of the, protein had not been assigned previously, and it is annotated as, hypothetical in sequence databases. The protein exhibits the, alpha/beta-hydrolase fold (also termed the Rossmann fold) and resembles, most closely the fold of the L-2-haloacid dehalogenase (HAD) superfamily., Following this observation, a detailed sequence analysis revealed remote, homology to two members of the HAD superfamily, the P-domain of Ca(2+), ATPase and phosphoserine phosphatase. The 19-kDa chains of HI1679 form a, tetramer both in solution and in the crystalline form. The four monomers, are arranged in a ring such that four beta-hairpin loops, each inserted, after the first beta-strand of the core alpha/beta-fold, form an, eight-stranded barrel at the center of the assembly. Four active sites are, located at the subunit interfaces. Each active site is occupied by a, cobalt ion, a metal used for crystallization. The cobalt is octahedrally, coordinated to two aspartate side-chains, a backbone oxygen, and three, solvent molecules, indicating that the physiological metal may be, magnesium. HI1679 hydrolyzes a number of phosphates, including, 6-phosphogluconate and phosphotyrosine, suggesting that it functions as a, phosphatase in vivo. The physiological substrate is yet to be identified;, however the location of the gene on the yrb operon suggests involvement in, sugar metabolism.
+The crystal structure of the YrbI protein from Haemophilus influenzae (HI1679) was determined at a 1.67-A resolution. The function of the protein had not been assigned previously, and it is annotated as hypothetical in sequence databases. The protein exhibits the alpha/beta-hydrolase fold (also termed the Rossmann fold) and resembles most closely the fold of the L-2-haloacid dehalogenase (HAD) superfamily. Following this observation, a detailed sequence analysis revealed remote homology to two members of the HAD superfamily, the P-domain of Ca(2+) ATPase and phosphoserine phosphatase. The 19-kDa chains of HI1679 form a tetramer both in solution and in the crystalline form. The four monomers are arranged in a ring such that four beta-hairpin loops, each inserted after the first beta-strand of the core alpha/beta-fold, form an eight-stranded barrel at the center of the assembly. Four active sites are located at the subunit interfaces. Each active site is occupied by a cobalt ion, a metal used for crystallization. The cobalt is octahedrally coordinated to two aspartate side-chains, a backbone oxygen, and three solvent molecules, indicating that the physiological metal may be magnesium. HI1679 hydrolyzes a number of phosphates, including 6-phosphogluconate and phosphotyrosine, suggesting that it functions as a phosphatase in vivo. The physiological substrate is yet to be identified; however the location of the gene on the yrb operon suggests involvement in sugar metabolism.
 ==About this Structure==
-J8D 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 GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1J8D OCA].
+J8D 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=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J8D OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Herzberg, O.]]
 [[Category: Lim, K.]]
-[[Category: S2F, Structure.2.Function.Project.]]
+[[Category: S2F, Structure 2.Function Project.]]
 [[Category: GOL]]
 [[Category: hi1679]]
@@ Line 23: / Line 23: @@
 [[Category: structure 2 function project]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:00:36 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:19:52 2008''