1lby

From Proteopedia

(Difference between revisions)

Revision as of 07:58, 25 November 2020

Crystal Structure of a complex (P32 crystal form) of dual activity FBPase/IMPase (AF2372) from Archaeoglobus fulgidus with 3 Manganese ions, Fructose-6-Phosphate, and Phosphate ion

Structural highlights

1lby is a 2 chain structure with sequence from Arcfl. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1lbv, 1lbw, 1lbx, 1lbz
Gene:	AF2372 (ARCFL)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[BSUHB_ARCFU] Phosphatase with broad specificity; it can dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of inositol-1-phosphate (I-1-P), 2'-AMP, pNPP, inositol-2-phosphate, beta-glycerol phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze glucose-6-phosphate and fructose-6-phosphate. May be involved in the biosynthesis of a unique osmolyte, di-myo-inositol 1,1-phosphate.^[1] ^[2] ^[3]

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

Several hyperthermophilic organisms contain an unusual phosphatase that has dual activity toward inositol monophosphates and fructose 1,6-bisphosphate. The structure of the second member of this family, an FBPase/IMPase from Archaeoglobus fulgidus (AF2372), has been solved. This enzyme shares many kinetic and structural similarities with that of a previously solved enzyme from Methanococcus jannaschii (MJ0109). It also shows some kinetic differences in divalent metal ion binding as well as structural variations at the dimer interface that correlate with decreased thermal stability. The availability of different crystal forms allowed us to investigate the effect of the presence of ligands on the conformation of a mobile catalytic loop independently of the crystal packing. This conformational variability in AF2372 is compared with that observed in other members of this structural family that are sensitive or insensitive to submillimolar concentrations of Li(+). This analysis provides support for the previously proposed mechanism of catalysis involving three metal ions. A direct correlation of the loop conformation with strength of Li(+) inhibition provides a useful system of classification for this extended family of enzymes.

Crystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. The story of a mobile loop.,Stieglitz KA, Johnson KA, Yang H, Roberts MF, Seaton BA, Head JF, Stec B J Biol Chem. 2002 Jun 21;277(25):22863-74. Epub 2002 Apr 8. PMID:11940584^[4]

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

References

↑ Chen L, Roberts MF. Overexpression, purification, and analysis of complementation behavior of E. coli SuhB protein: comparison with bacterial and archaeal inositol monophosphatases. Biochemistry. 2000 Apr 11;39(14):4145-53. PMID:10747806
↑ Stec B, Yang H, Johnson KA, Chen L, Roberts MF. MJ0109 is an enzyme that is both an inositol monophosphatase and the 'missing' archaeal fructose-1,6-bisphosphatase. Nat Struct Biol. 2000 Nov;7(11):1046-50. PMID:11062561 doi:10.1038/80968
↑ Stieglitz KA, Johnson KA, Yang H, Roberts MF, Seaton BA, Head JF, Stec B. Crystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. The story of a mobile loop. J Biol Chem. 2002 Jun 21;277(25):22863-74. Epub 2002 Apr 8. PMID:11940584 doi:http://dx.doi.org/10.1074/jbc.M201042200
↑ Stieglitz KA, Johnson KA, Yang H, Roberts MF, Seaton BA, Head JF, Stec B. Crystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. The story of a mobile loop. J Biol Chem. 2002 Jun 21;277(25):22863-74. Epub 2002 Apr 8. PMID:11940584 doi:http://dx.doi.org/10.1074/jbc.M201042200

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Crystal Structure of a complex (P32 crystal form) of dual activity FBPase/IMPase (AF2372) from Archaeoglobus fulgidus with 3 Manganese ions, Fructose-6-Phosphate, and Phosphate ion==
-<StructureSection load='1lby' size='340' side='right' caption='[[1lby]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
+<StructureSection load='1lby' size='340' side='right'caption='[[1lby]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1lby]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfl Arcfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LBY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LBY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1lby]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfl Arcfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LBY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1LBY FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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">[[1lbv|1lbv]], [[1lbw|1lbw]], [[1lbx|1lbx]], [[1lbz|1lbz]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1lbv|1lbv]], [[1lbw|1lbw]], [[1lbx|1lbx]], [[1lbz|1lbz]]</div></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AF2372 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2234 ARCFL])</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=1lby FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lby OCA], [http://pdbe.org/1lby PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lby RCSB], [http://www.ebi.ac.uk/pdbsum/1lby PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lby 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=1lby FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lby OCA], [http://pdbe.org/1lby PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lby RCSB], [http://www.ebi.ac.uk/pdbsum/1lby PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lby ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 30: / Line 30: @@
 </div>
 <div class="pdbe-citations 1lby" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Inositol monophosphatase 3D structures|Inositol monophosphatase 3D structures]]
 == References ==
 <references/>
@@ Line 35: / Line 38: @@
 </StructureSection>
 [[Category: Arcfl]]
+[[Category: Large Structures]]
 [[Category: Head, J F]]
 [[Category: Johnson, K A]]

1lby

From Proteopedia

Revision as of 07:58, 25 November 2020

Crystal Structure of a complex (P32 crystal form) of dual activity FBPase/IMPase (AF2372) from Archaeoglobus fulgidus with 3 Manganese ions, Fructose-6-Phosphate, and Phosphate ion

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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