From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1k1e.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1k1e.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1k1e| PDB=1k1e | SCENE= }} | | {{STRUCTURE_1k1e| PDB=1k1e | SCENE= }} |
| | | | |
| - | '''Structure Of the cobalt-bound form of the deoxy-D-mannose-octulosonate 8-phosphate phosphatase (YrbI) From Haemophilus Influenzae (HI1679)'''
| + | ===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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_11835514}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11835514 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_11835514}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 30: |
Line 34: |
| | [[Category: Structural genomic]] | | [[Category: Structural genomic]] |
| | [[Category: Structure 2 function project]] | | [[Category: Structure 2 function project]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:10:45 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 21:16:30 2008'' |
Revision as of 18:16, 1 July 2008
Template:STRUCTURE 1k1e
Structure Of the cobalt-bound form of the deoxy-D-mannose-octulosonate 8-phosphate phosphatase (YrbI) From Haemophilus Influenzae (HI1679)
Template:ABSTRACT PUBMED 11835514
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
Page seeded by OCA on Tue Jul 1 21:16:30 2008
