1l5x

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|PDB= 1l5x |SIZE=350|CAPTION= <scene name='initialview01'>1l5x</scene>, resolution 2.00&Aring;
|PDB= 1l5x |SIZE=350|CAPTION= <scene name='initialview01'>1l5x</scene>, resolution 2.00&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene>
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|LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= PAE2908 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=13773 Pyrobaculum aerophilum])
|GENE= PAE2908 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=13773 Pyrobaculum aerophilum])
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|DOMAIN=
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|RELATEDENTRY=[[1j9j|1J9J]], [[1ilv|1ILV]], [[1j9l|1J9L]], [[1j9k|1J9K]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l5x OCA], [http://www.ebi.ac.uk/pdbsum/1l5x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l5x RCSB]</span>
}}
}}
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[[Category: Katz, J E.]]
[[Category: Katz, J E.]]
[[Category: Mura, C.]]
[[Category: Mura, C.]]
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[[Category: ACY]]
 
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[[Category: GOL]]
 
[[Category: mixed alpha/beta protein]]
[[Category: mixed alpha/beta protein]]
[[Category: n-terminal rossmann-fold like]]
[[Category: n-terminal rossmann-fold like]]
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[[Category: structural genomic]]
[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:26:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:58:34 2008''

Revision as of 18:58, 30 March 2008


PDB ID 1l5x

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands: , ,
Gene: PAE2908 (Pyrobaculum aerophilum)
Related: 1J9J, 1ILV, 1J9L, 1J9K


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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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