1jmv
From Proteopedia
(New page: 200px<br /><applet load="1jmv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jmv, resolution 1.85Å" /> '''Structure of Haemoph...) |
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| - | [[Image:1jmv.gif|left|200px]]<br /><applet load="1jmv" size=" | + | [[Image:1jmv.gif|left|200px]]<br /><applet load="1jmv" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jmv, resolution 1.85Å" /> | caption="1jmv, resolution 1.85Å" /> | ||
'''Structure of Haemophylus influenzae Universal Stress Protein At 1.85A Resolution'''<br /> | '''Structure of Haemophylus influenzae Universal Stress Protein At 1.85A Resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: The universal stress protein UspA is a small cytoplasmic | + | BACKGROUND: The universal stress protein UspA is a small cytoplasmic bacterial protein whose expression is enhanced several-fold when cellular viability is challenged with heat shock, nutrient starvation, stress agents which arrest cell growth, or DNA-damaging agents. UspA enhances the rate of cell survival during prolonged exposure to such conditions, suggesting that it asserts a general "stress endurance" activity. However, neither the structure of UspA nor the biochemical mechanism by which it protects cells from the broad spectrum of stress agents is known. RESULTS: The crystal structure of Haemophilus influenzae UspA reveals an asymmetric dimer with a tertiary alpha/beta fold similar to that of the Methanococcus jannaschi MJ0577 protein, a protein whose crystal structure revealed a novel ATP binding motif. UspA differs significantly from the MJ0577 structure in several details, including the triphosphate binding loop of the ATP binding motif; UspA shows no ATP binding activity. CONCLUSIONS: Within the universal stress protein family that is delineated by sequence similarity, UspA is the only member which has been correlated with a cellular activity, and MJ0577 is the only member which has been assigned a biochemical activity, i.e., ATP binding. UspA has a similar fold to the MJ0577 protein but does not bind ATP. This suggests that members of this protein family will segregate into two groups, based on whether or not they bind ATP. By implication, one subset of the universal stress proteins presumably has an ATP-dependent function, while another subset functions in ATP-independent activities. |
==About this Structure== | ==About this Structure== | ||
| - | 1JMV 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 SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1JMV 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=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JMV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Haemophilus influenzae]] | [[Category: Haemophilus influenzae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: McKay, D | + | [[Category: McKay, D B.]] |
| - | [[Category: Sousa, M | + | [[Category: Sousa, M C.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: universal stress protein]] | [[Category: universal stress protein]] | ||
[[Category: uspa]] | [[Category: uspa]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:24:24 2008'' |
Revision as of 11:24, 21 February 2008
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Structure of Haemophylus influenzae Universal Stress Protein At 1.85A Resolution
Overview
BACKGROUND: The universal stress protein UspA is a small cytoplasmic bacterial protein whose expression is enhanced several-fold when cellular viability is challenged with heat shock, nutrient starvation, stress agents which arrest cell growth, or DNA-damaging agents. UspA enhances the rate of cell survival during prolonged exposure to such conditions, suggesting that it asserts a general "stress endurance" activity. However, neither the structure of UspA nor the biochemical mechanism by which it protects cells from the broad spectrum of stress agents is known. RESULTS: The crystal structure of Haemophilus influenzae UspA reveals an asymmetric dimer with a tertiary alpha/beta fold similar to that of the Methanococcus jannaschi MJ0577 protein, a protein whose crystal structure revealed a novel ATP binding motif. UspA differs significantly from the MJ0577 structure in several details, including the triphosphate binding loop of the ATP binding motif; UspA shows no ATP binding activity. CONCLUSIONS: Within the universal stress protein family that is delineated by sequence similarity, UspA is the only member which has been correlated with a cellular activity, and MJ0577 is the only member which has been assigned a biochemical activity, i.e., ATP binding. UspA has a similar fold to the MJ0577 protein but does not bind ATP. This suggests that members of this protein family will segregate into two groups, based on whether or not they bind ATP. By implication, one subset of the universal stress proteins presumably has an ATP-dependent function, while another subset functions in ATP-independent activities.
About this Structure
1JMV is a Single protein structure of sequence from Haemophilus influenzae with as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the universal stress protein of Haemophilus influenzae., Sousa MC, McKay DB, Structure. 2001 Dec;9(12):1135-41. PMID:11738040
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