2g1a: Difference between revisions

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-[[Image:2g1a.jpg|left|200px]]<br /><applet load="2g1a" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="2g1a, resolution 2.00&Aring;" />
-'''Crystal structure of the complex between Apha class B acid phosphatase/phosphotransferase'''<br />
-==Overview==
+==Crystal structure of the complex between Apha class B acid phosphatase/phosphotransferase==
-AphA is a periplasmic acid phosphatase of Escherichia coli belonging to, class B bacterial phosphatases, which is part of the DDDD superfamily of, phosphohydrolases. The crystal structure of AphA has been determined at, 2.2A and its resolution extended to 1.7A on an AuCl(3) derivative. This, represents the first crystal structure of a class B bacterial phosphatase., Despite the lack of sequence homology, the AphA structure reveals a, haloacid dehalogenase-like fold. This finding suggests that this fold, could be conserved among members of the DDDD superfamily of, phosphohydrolases. The active enzyme is a homotetramer built by using an, extended N-terminal arm intertwining the four monomers. The active site of, the native enzyme, as prepared, hosts a magnesium ion, which can be, replaced by other metal ions. The structure explains the non-specific, behaviour of AphA towards substrates, while a structure-based alignment, with other phosphatases provides clues about the catalytic mechanism.
+<StructureSection load='2g1a' size='340' side='right'caption='[[2g1a]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2g1a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G1A FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5HG:{[2-(6-AMINO-9H-PURIN-9-YL)ETHOXY]METHYL}PHOSPHONIC+ACID'>5HG</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2g1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g1a OCA], [https://pdbe.org/2g1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g1a RCSB], [https://www.ebi.ac.uk/pdbsum/2g1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g1a ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/APHA_ECOLI APHA_ECOLI] Dephosphorylates several organic phosphate monoesters including 3'- and 5'-nucleotides, 2'-deoxy-5'-nucleotides, pNPP, phenyl phosphate, glycerol 2-phosphate, ribose 5-phosphate, O-phospho-L-amino acids and phytic acid, showing the highest activity with aryl phosphoesters (pNPP, phenyl phosphate and O-phospho-L-tyrosine), and to a lesser extent with 3'- and 5'-nucleotides. No activity toward ATP, phosphodiesters, glycerol-1-phosphate, glucose 1-phosphate, glucose 6-phosphate, NADP, GTP or 3',5'-cAMP, ADP or ATP. 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. Capable of transferring phosphate from either pNPP or UMP to adenosine or uridine. Does not exhibit nucleotide phosphomutase activity.<ref>PMID:9011040</ref> <ref>PMID:16297670</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g1/2g1a_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <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/main_output.php?pdb_ID=2g1a ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-G1A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=5HG:'>5HG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G1A OCA].
+*[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]]
+== References ==
-==Reference==
+<references/>
-The first structure of a bacterial class B Acid phosphatase reveals further structural heterogeneity among phosphatases of the haloacid dehalogenase fold., Calderone V, Forleo C, Benvenuti M, Cristina Thaller M, Maria Rossolini G, Mangani S, J Mol Biol. 2004 Jan 16;335(3):761-73. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14687572 14687572]
+__TOC__
-[[Category: Acid phosphatase]]
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Benvenuti, M.]]
+[[Category: Benvenuti M]]
-[[Category: Calderone, V.]]
+[[Category: Calderone V]]
-[[Category: Cappelletti, E.]]
+[[Category: Cappelletti E]]
-[[Category: Leone, R.]]
+[[Category: Leone R]]
-[[Category: Mangani, S.]]
+[[Category: Mangani S]]
-[[Category: 5HG]]
-[[Category: MG]]
-[[Category: hydrolase; acid phosphatase/phosphotransferase; metallo phosphatase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:34:25 2008''