1k1e
From Proteopedia
(New page: 200px<br /><applet load="1k1e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k1e, resolution 1.67Å" /> '''Structure Of the cob...) |
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| - | [[Image:1k1e.gif|left|200px]]<br /><applet load="1k1e" size=" | + | [[Image:1k1e.gif|left|200px]]<br /><applet load="1k1e" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1k1e, resolution 1.67Å" /> | caption="1k1e, resolution 1.67Å" /> | ||
'''Structure Of the cobalt-bound form of the deoxy-D-mannose-octulosonate 8-phosphate phosphatase (YrbI) From Haemophilus Influenzae (HI1679)'''<br /> | '''Structure Of the cobalt-bound form of the deoxy-D-mannose-octulosonate 8-phosphate phosphatase (YrbI) From Haemophilus Influenzae (HI1679)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the YrbI protein from Haemophilus influenzae | + | 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== | ==About this Structure== | ||
| - | 1K1E 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 CO, HG, SO4, MES and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1K1E 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=CO:'>CO</scene>, <scene name='pdbligand=HG:'>HG</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=MES:'>MES</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K1E OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Herzberg, O.]] | [[Category: Herzberg, O.]] | ||
[[Category: Lim, K.]] | [[Category: Lim, K.]] | ||
| - | [[Category: S2F, Structure | + | [[Category: S2F, Structure 2.Function Project.]] |
[[Category: CO]] | [[Category: CO]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
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[[Category: structure 2 function project]] | [[Category: structure 2 function project]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:29:01 2008'' |
Revision as of 11:29, 21 February 2008
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Structure Of the cobalt-bound form of the deoxy-D-mannose-octulosonate 8-phosphate phosphatase (YrbI) From Haemophilus Influenzae (HI1679)
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.
About this Structure
1K1E is a Single protein structure of sequence from Haemophilus influenzae with , , , and as ligands. Full crystallographic information is available from OCA.
Reference
From structure to function: YrbI from Haemophilus influenzae (HI1679) is a phosphatase., Parsons JF, Lim K, Tempczyk A, Krajewski W, Eisenstein E, Herzberg O, Proteins. 2002 Mar 1;46(4):393-404. PMID:11835514
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