1l5x
From Proteopedia
(New page: 200px<br /><applet load="1l5x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l5x, resolution 2.00Å" /> '''The 2.0-Angstrom res...) |
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| - | [[Image:1l5x.jpg|left|200px]]<br /><applet load="1l5x" size=" | + | [[Image:1l5x.jpg|left|200px]]<br /><applet load="1l5x" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1l5x, resolution 2.00Å" /> | caption="1l5x, resolution 2.00Å" /> | ||
'''The 2.0-Angstrom resolution crystal structure of a survival protein E (SurE) homolog from Pyrobaculum aerophilum'''<br /> | '''The 2.0-Angstrom resolution crystal structure of a survival protein E (SurE) homolog from Pyrobaculum aerophilum'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The survival protein E (SurE) family was discovered by its correlation to | + | The survival protein E (SurE) family was discovered by its correlation to stationary phase survival of Escherichia coli and various repair proteins involved in sustaining this and other stress-response phenotypes. In order to better understand this ancient and well-conserved protein family, we have determined the 2.0A resolution crystal structure of SurEalpha from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum (Pae). This first structure of an archaeal SurE reveals significant similarities to and differences from the only other known SurE structure, that from the eubacterium Thermatoga maritima (Tma). Both SurE monomers adopt similar folds; however, unlike the Tma SurE dimer, crystalline Pae SurEalpha is predominantly non-domain swapped. Comparative structural analyses of Tma and Pae SurE suggest conformationally variant regions, such as a hinge loop that may be involved in domain swapping. The putative SurE active site is highly conserved, and implies a model for SurE bound to a potential substrate, guanosine-5'-monophosphate (GMP). Pae SurEalpha has optimal acid phosphatase activity at temperatures above 90 degrees C, and is less specific than Tma SurE in terms of metal ion requirements. Substrate specificity also differs between Pae and Tma SurE, with a more specific recognition of purine nucleotides by the archaeal enzyme. Analyses of the sequences, phylogenetic distribution, and genomic organization of the SurE family reveal examples of genomes encoding multiple surE genes, and suggest that SurE homologs constitute a broad family of enzymes with phosphatase-like activities. |
==About this Structure== | ==About this Structure== | ||
| - | 1L5X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum] with GOL and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1L5X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum] with <scene name='pdbligand=GOL:'>GOL</scene> and <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L5X OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Pyrobaculum aerophilum]] | [[Category: Pyrobaculum aerophilum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Clarke, S | + | [[Category: Clarke, S G.]] |
[[Category: Eisenberg, D.]] | [[Category: Eisenberg, D.]] | ||
| - | [[Category: Katz, J | + | [[Category: Katz, J E.]] |
[[Category: Mura, C.]] | [[Category: Mura, C.]] | ||
[[Category: ACY]] | [[Category: ACY]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:41:46 2008'' |
Revision as of 11:41, 21 February 2008
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The 2.0-Angstrom resolution crystal structure of a survival protein E (SurE) homolog from Pyrobaculum aerophilum
Overview
The survival protein E (SurE) family was discovered by its correlation to stationary phase survival of Escherichia coli and various repair proteins involved in sustaining this and other stress-response phenotypes. In order to better understand this ancient and well-conserved protein family, we have determined the 2.0A resolution crystal structure of SurEalpha from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum (Pae). This first structure of an archaeal SurE reveals significant similarities to and differences from the only other known SurE structure, that from the eubacterium Thermatoga maritima (Tma). Both SurE monomers adopt similar folds; however, unlike the Tma SurE dimer, crystalline Pae SurEalpha is predominantly non-domain swapped. Comparative structural analyses of Tma and Pae SurE suggest conformationally variant regions, such as a hinge loop that may be involved in domain swapping. The putative SurE active site is highly conserved, and implies a model for SurE bound to a potential substrate, guanosine-5'-monophosphate (GMP). Pae SurEalpha has optimal acid phosphatase activity at temperatures above 90 degrees C, and is less specific than Tma SurE in terms of metal ion requirements. Substrate specificity also differs between Pae and Tma SurE, with a more specific recognition of purine nucleotides by the archaeal enzyme. Analyses of the sequences, phylogenetic distribution, and genomic organization of the SurE family reveal examples of genomes encoding multiple surE genes, and suggest that SurE homologs constitute a broad family of enzymes with phosphatase-like activities.
About this Structure
1L5X is a Single protein structure of sequence from Pyrobaculum aerophilum with and as ligands. Full crystallographic information is available from OCA.
Reference
Structure and function of an archaeal homolog of survival protein E (SurEalpha): an acid phosphatase with purine nucleotide specificity., Mura C, Katz JE, Clarke SG, Eisenberg D, J Mol Biol. 2003 Mar 7;326(5):1559-75. PMID:12595266
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