1k1e
From Proteopedia
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|PDB= 1k1e |SIZE=350|CAPTION= <scene name='initialview01'>1k1e</scene>, resolution 1.67Å | |PDB= 1k1e |SIZE=350|CAPTION= <scene name='initialview01'>1k1e</scene>, resolution 1.67Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= HI1679 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae]) | |GENE= HI1679 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1j8d|1j8d]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k1e OCA], [http://www.ebi.ac.uk/pdbsum/1k1e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k1e RCSB]</span> | ||
}} | }} | ||
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[[Category: Lim, K.]] | [[Category: Lim, K.]] | ||
[[Category: S2F, Structure 2.Function Project.]] | [[Category: S2F, Structure 2.Function Project.]] | ||
- | [[Category: CO]] | ||
- | [[Category: GOL]] | ||
- | [[Category: HG]] | ||
- | [[Category: MES]] | ||
- | [[Category: SO4]] | ||
[[Category: hi1679]] | [[Category: hi1679]] | ||
[[Category: kdo 8-p phosphatase]] | [[Category: kdo 8-p phosphatase]] | ||
Line 36: | Line 34: | ||
[[Category: structure 2 function project]] | [[Category: structure 2 function project]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:41:54 2008'' |
Revision as of 18:41, 30 March 2008
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, resolution 1.67Å | |||||||
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Ligands: | , , , , | ||||||
Gene: | HI1679 (Haemophilus influenzae) | ||||||
Related: | 1j8d
| ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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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