1z88

From Proteopedia

(Difference between revisions)

Revision as of 15:30, 12 October 2017

Crystal structure of Lys154Arg mutant of mature AphA of S. typhimurium

Structural highlights

1z88 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1z5g, 1z5u
Activity:	Acid phosphatase, with EC number 3.1.3.2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[APHA_SALTY] Dephosphorylates several organic phosphate monoesters such as 3'-UMP, 5'-UMP and pNPP. Also has a phosphotransferase activity catalyzing the transfer of low-energy phosphate groups from organic phosphate monoesters to free hydroxyl groups of various organic compounds such as the 2'-, 3-, or 5'-hydroxyls of nucleosides and nucleotides. Also displays significant phosphomutase activity since it is able to catalyze the transfer of the phosphate group of 3'-AMP from the 3'-position both to the 2'- and 5'-positions. One of the physiological functions of the phosphohydrolytic activity of the enzyme is believed to be the scavenging of organic phosphate esters that otherwise cannot pass the cytoplasmic membrane.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The Salmonella typhimurium class B nonspecific acid phosphatase (AphA protein) belongs to the L2-haloacid dehalogenase superfamily. The conserved Lys-154 interacts with substrate phosphate, nucleophile Asp-46, and Asp-173 in the wild-type AphA protein. Asp-173 also interacts with Mg(II) water ligand and with main-chain amide of loop-4. We report here the mutational analysis of Lys-154 and Asp-173, the crystal structures of the K154N and K154R mutants, and the results of electrostatic potential calculations. The K154N, K154R and D173N mutants display significant reduction in the phosphatase activity. Lys-154 may not be responsible for a juxtaposition of the substrate phosphate and the aspartyl nucleophile, but has an hitherto unknown functional role of rendering the substrate phosphorous atom electron deficient. Nearly 10,000-fold increase in the K(d) value for dissociation of the cofactor Mg(II) observed for the D173N mutant correlates well with theoretically estimated change in the binding free energy of Mg(II).

Structural and mutational analyses reveal the functional role of active-site Lys-154 and Asp-173 of Salmonella typhimurium AphA protein.,Makde RD, Gupta GD, Mahajan SK, Kumar V Arch Biochem Biophys. 2007 Aug 1;464(1):70-9. Epub 2007 May 30. PMID:17570338^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Uerkvitz W, Beck CF. Periplasmic phosphatases in Salmonella typhimurium LT2. A biochemical, physiological, and partial genetic analysis of three nucleoside monophosphate dephosphorylating enzymes. J Biol Chem. 1981 Jan 10;256(1):382-9. PMID:6256351
↑ Uerkvitz W. Periplasmic nonspecific acid phosphatase II from Salmonella typhimurium LT2. Crystallization, detergent reactivation, and phosphotransferase activity. J Biol Chem. 1988 Oct 25;263(30):15823-30. PMID:3049613
↑ Makde RD, Gupta GD, Mahajan SK, Kumar V. Structural and mutational analyses reveal the functional role of active-site Lys-154 and Asp-173 of Salmonella typhimurium AphA protein. Arch Biochem Biophys. 2007 Aug 1;464(1):70-9. Epub 2007 May 30. PMID:17570338 doi:10.1016/j.abb.2007.03.043

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1z88"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Lys154Arg mutant of mature AphA of S. typhimurium==
 <StructureSection load='1z88' size='340' side='right' caption='[[1z88]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1z5g|1z5g]], [[1z5u|1z5u]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1z88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z88 OCA], [http://pdbe.org/1z88 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z88 RCSB], [http://www.ebi.ac.uk/pdbsum/1z88 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1z88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z88 OCA], [http://pdbe.org/1z88 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z88 RCSB], [http://www.ebi.ac.uk/pdbsum/1z88 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z88 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1z88 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

1z88

From Proteopedia

Revision as of 15:30, 12 October 2017

Crystal structure of Lys154Arg mutant of mature AphA of S. typhimurium

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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