1fbh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1fbh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fbh, resolution 2.5&Aring;" /> '''CRYSTALLOGRAPHIC STUD...)
Current revision (07:12, 7 February 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1fbh.jpg|left|200px]]<br /><applet load="1fbh" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1fbh, resolution 2.5&Aring;" />
 
-
'''CRYSTALLOGRAPHIC STUDIES OF THE CATALYTIC MECHANISM OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE'''<br />
 
-
==Overview==
+
==CRYSTALLOGRAPHIC STUDIES OF THE CATALYTIC MECHANISM OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE==
-
The crystal structures of fructose-1,6-bisphosphatase (EC 3.1.3.11), complexed with substrate alone or with substrate analogues in the presence, of divalent metal ions have been determined. The substrate analogues, 2,5-anhydro-D-glucitol-1,6-bisphosphate (AhG-1,6-P2) and, 2,5-anhydro-D-mannitol-1,6-bisphosphate (AhM-1,6-P2), differ from the, alpha and beta anomers of fructose-1,6-bisphosphate (Fru-1,6-P2), respectively, in that the OH on C2 is replaced by a hydrogen atom., Structures have been refined at resolutions of 2.5 to 3.0 A to R factors, of 0.172 to 0.195 with root-mean-square deviations of 0.012-0.018 A and, 2.7-3.8 degrees from the ideal geometries of bond lengths and bond angles, respectively. In addition, the complex of substrate with the enzyme has, been determined in the absence of metal. The electron density at 2.5-A, resolution does not distinguish between alpha and beta anomers, which, differ for the most part only in the position of the 1-phosphate group and, the orientation of the C2-hydroxyl group. The positions of the 6-phosphate, and the sugar ring of the substrate analogues are almost identical to, those of the respective anomer of the substrate. In the presence of metal, ions the positions of the 1-phosphate groups of both alpha and beta, analogues differ significantly (0.8-1.0 A) from those of anomers of the, substrate in the metal-free complex. Two metal ions (Mn2+ or Zn2+) are, located at the enzyme active site of complexes of the alpha analogue, AhG-1,6-P2. Metal site 1 is coordinated by the carboxylate groups of, Glu-97, Asp-118, and Glu-280 and the 1-phosphate group of substrate, analogue, while the metal site 2 is coordinated by the carboxylate groups, of Glu-97, Asp-118, the 1-phosphate group of substrate analogue, and the, carbonyl oxygen of Leu-120. Both metal sites have a distorted tetrahedral, geometry. However, only one metal ion (Mg2+ or Mn2+) is found very near, the metal site 1 in the enzyme's active site in complexes of the beta, analogue AhM-1,6-P2 or for Mg2+ in the complex of the alpha analogue, AhG-1,6-P2. This single metal ion is coordinated by the carboxylate groups, of Glu-97, Asp-118, Asp-121, and Glu-280 and the 1-phosphate group of, substrate analogue in a distorted square pyramidal geometry.(ABSTRACT, TRUNCATED AT 400 WORDS)
+
<StructureSection load='1fbh' size='340' side='right'caption='[[1fbh]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1fbh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FBH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FBH 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]] 2.5&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AFP:ALPHA+FRUCTOSE+1,6-DIPHOSPHATE'>AFP</scene>, <scene name='pdbligand=FBP:BETA-FRUCTOSE-1,6-DIPHOSPHATE'>FBP</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=1fbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fbh OCA], [https://pdbe.org/1fbh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fbh RCSB], [https://www.ebi.ac.uk/pdbsum/1fbh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fbh ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/F16P1_PIG F16P1_PIG]
 +
== 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/fb/1fbh_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=1fbh ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1FBH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Active as [http://en.wikipedia.org/wiki/Fructose-bisphosphatase Fructose-bisphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.11 3.1.3.11] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FBH OCA].
+
*[[Fructose-1%2C6-bisphosphatase 3D structures|Fructose-1%2C6-bisphosphatase 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
Crystallographic studies of the catalytic mechanism of the neutral form of fructose-1,6-bisphosphatase., Zhang Y, Liang JY, Huang S, Ke H, Lipscomb WN, Biochemistry. 1993 Feb 23;32(7):1844-57. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8382525 8382525]
+
[[Category: Large Structures]]
-
[[Category: Fructose-bisphosphatase]]
+
-
[[Category: Single protein]]
+
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
-
[[Category: Huang, S.]]
+
[[Category: Huang S]]
-
[[Category: Ke, H.]]
+
[[Category: Ke H]]
-
[[Category: Liang, J.Y.]]
+
[[Category: Liang J-Y]]
-
[[Category: Lipscomb, W.N.]]
+
[[Category: Lipscomb WN]]
-
[[Category: Zhang, Y.]]
+
[[Category: Zhang Y]]
-
[[Category: hydrolase(phosphoric monoester)]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:47:29 2007''
+

Current revision

CRYSTALLOGRAPHIC STUDIES OF THE CATALYTIC MECHANISM OF THE NEUTRAL FORM OF FRUCTOSE-1,6-BISPHOSPHATASE

PDB ID 1fbh

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fbh"
Personal tools