1rmy: Difference between revisions

Revision as of 13:30, 16 December 2020

Crystal structure of AphA class B acid phosphatase/phosphotransferase ternary complex with deoxycytosine and phosphate bound to the catalytic metal

Structural highlights

1rmy is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	DCZ, MG, PO4
Related:	1n8n, 1n9k, 1rm7, 1rmq, 1rmt, 1rmw
Gene:	APHA, NAPA, B4055, SF4149, S3580 ("Bacillus coli" Migula 1895)
Activity:	Acid phosphatase, with EC number 3.1.3.2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2]

Evolutionary Conservation

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

References

↑ Thaller MC, Schippa S, Bonci A, Cresti S, Rossolini GM. Identification of the gene (aphA) encoding the class B acid phosphatase/phosphotransferase of Escherichia coli MG1655 and characterization of its product. FEMS Microbiol Lett. 1997 Jan 15;146(2):191-8. PMID:9011040
↑ Passariello C, Forleo C, Micheli V, Schippa S, Leone R, Mangani S, Thaller MC, Rossolini GM. Biochemical characterization of the class B acid phosphatase (AphA) of Escherichia coli MG1655. Biochim Biophys Acta. 2006 Jan;1764(1):13-9. Epub 2005 Nov 2. PMID:16297670 doi:https://dx.doi.org/10.1016/j.bbapap.2005.08.028

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OCA

[1] Thaller MC, Schippa S, Bonci A, Cresti S, Rossolini GM. Identification of the gene (aphA) encoding the class B acid phosphatase/phosphotransferase of Escherichia coli MG1655 and characterization of its product. FEMS Microbiol Lett. 1997 Jan 15;146(2):191-8. PMID:9011040

[2] Passariello C, Forleo C, Micheli V, Schippa S, Leone R, Mangani S, Thaller MC, Rossolini GM. Biochemical characterization of the class B acid phosphatase (AphA) of Escherichia coli MG1655. Biochim Biophys Acta. 2006 Jan;1764(1):13-9. Epub 2005 Nov 2. PMID:16297670 doi:https://dx.doi.org/10.1016/j.bbapap.2005.08.028

[1]

[2]

@@ Line 1: / Line 1: @@
 ==Crystal structure of AphA class B acid phosphatase/phosphotransferase ternary complex with deoxycytosine and phosphate bound to the catalytic metal==
-<StructureSection load='1rmy' size='340' side='right' caption='[[1rmy]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+<StructureSection load='1rmy' size='340' side='right'caption='[[1rmy]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1rmy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RMY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RMY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1rmy]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RMY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1RMY FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DCZ:2-DEOXYCYTIDINE'>DCZ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DCZ:2-DEOXYCYTIDINE'>DCZ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1n8n|1n8n]], [[1n9k|1n9k]], [[1rm7|1rm7]], [[1rmq|1rmq]], [[1rmt|1rmt]], [[1rmw|1rmw]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1n8n|1n8n]], [[1n9k|1n9k]], [[1rm7|1rm7]], [[1rmq|1rmq]], [[1rmt|1rmt]], [[1rmw|1rmw]]</div></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">APHA, NAPA, B4055, SF4149, S3580 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=1rmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rmy OCA], [http://pdbe.org/1rmy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rmy RCSB], [http://www.ebi.ac.uk/pdbsum/1rmy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rmy ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1rmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rmy OCA], [http://pdbe.org/1rmy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rmy RCSB], [http://www.ebi.ac.uk/pdbsum/1rmy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rmy ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 24: / Line 24: @@
 ==See Also==
-*[[Acid phosphatase|Acid phosphatase]]
+*[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]]
 == References ==
 <references/>
@@ Line 31: / Line 31: @@
 [[Category: Bacillus coli migula 1895]]
 [[Category: Acid phosphatase]]
+[[Category: Large Structures]]
 [[Category: Benvenuti, M]]
 [[Category: Calderone, V]]

1rmy: Difference between revisions

Revision as of 13:30, 16 December 2020

Crystal structure of AphA class B acid phosphatase/phosphotransferase ternary complex with deoxycytosine and phosphate bound to the catalytic metal

Structural highlights

Function

Evolutionary Conservation

See Also

References

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