1faj: Difference between revisions

Revision as of 02:57, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1faj.png

1faj, resolution 2.15Å ()

Activity:

Inorganic diphosphatase, with EC number 3.6.1.1

Structural annotation:
Resources:	CATH : 1Faj000 InterPro : Ipr008162 Pfam : PF00719 SCOP : d1faj__ UniProt : P0A7A9

Functional annotation:
Cellular component:	cytoplasm membrane fraction
Biological process:	phosphate metabolic process
Molecular function:	hydrolase activity magnesium ion binding metal ion binding inorganic diphosphatase activity

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

INORGANIC PYROPHOSPHATASEINORGANIC PYROPHOSPHATASE

Template:ABSTRACT PUBMED 15299678

About this StructureAbout this Structure

1FAJ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structure of Escherichia coli inorganic pyrophosphatase at 2.2 A resolution., Kankare J, Salminen T, Lahti R, Cooperman BS, Baykov AA, Goldman A, Acta Crystallogr D Biol Crystallogr. 1996 May 1;52(Pt 3):551-63. PMID:15299678

Page seeded by OCA on Tue Jul 1 02:57:40 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_1faj|  PDB=1faj  |  SCENE=  }}
-'''INORGANIC PYROPHOSPHATASE'''
+===INORGANIC PYROPHOSPHATASE===
-==Overview==
+<!--
-The refined crystal structures of hexameric soluble inorganic pyrophosphatase from E. coli (E-PPase) are reported to R factors of 18.7 and 18.3% at 2.15 and 2.2 A, respectively. The first contains one independent monomer; the other, two independent monomers, in an R32 unit cell. Because the E-PPase monomer is small with a large open active site, there are relatively few hydrophobic interactions that connect the active-site loops to the five-stranded twisted beta-barrel that is the hydrophobic core of the molecule. The active-site loops are, however, held in place by interactions between monomers around the threefold and twofold symmetry axes of the D(3) hexamer. Consequently, mutations of active-site residues (such as Glu20 and Lysl04) often affect protein stability and oligomeric structure. Conversely, mutations of residues in the interface between monomers (such as His136 and Hisl40) not only affect oligomeric structure but also affect active-site function. The effects of the H136Q and H140Q variants can be explained by the extended ionic interaction between H140, D143 and H136' of the neighbouring monomer. This interaction is further buttressed by an extensive hydrogen-bonding network that appears to explain why the E-PPase hexamer is so stable and also why the H136Q and H140Q variant proteins are less stable as hexamers.
+The line below this paragraph, {{ABSTRACT_PUBMED_15299678}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15299678 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15299678}}
 ==About this Structure==
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 [[Category: Inorganic pyrophosphatase]]
 [[Category: Magnesium]]
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