This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1h2f

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:27, 27 March 2024) (edit) (undo)
 
(18 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1h2f.gif|left|200px]]<br />
 
-
<applet load="1h2f" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1h2f, resolution 2.00&Aring;" />
 
-
'''BACILLUS STEAROTHERMOPHILUS PHOE (PREVIOUSLY KNOWN AS YHFR) IN COMPLEX WITH TRIVANADATE'''<br />
 
-
==Overview==
+
==BACILLUS STEAROTHERMOPHILUS PHOE (previously known as yhfr) in complex with trivanadate==
-
Bacillus stearothermophilus phosphatase PhoE is a member of the, cofactor-dependent phosphoglycerate mutase superfamily possessing broad, specificity phosphatase activity. Its previous structural determination in, complex with glycerol revealed probable bases for its efficient hydrolysis, of both large, hydrophobic, and smaller, hydrophilic substrates. Here we, report two further structures of PhoE complexes, to higher resolution of, diffraction, which yield a better and thorough understanding of its, catalytic mechanism. The environment of the phosphate ion in the catalytic, site of the first complex strongly suggests an acid-base catalytic, function for Glu83. It also reveals how the C-terminal tail ordering is, linked to enzyme activation on phosphate binding by a different mechanism, to that seen in Escherichia coli phosphoglycerate mutase. The second, complex structure with an unusual doubly covalently bound trivanadate, shows how covalent modification of the phosphorylable His10 is accompanied, by small structural changes, presumably to catalytic advantage. When, compared with structures of related proteins in the cofactor-dependent, phosphoglycerate mutase superfamily, an additional phosphate ligand, Gln22, is observed in PhoE. Functional constraints lead to the, corresponding residue being conserved as Gly in, fructose-2,6-bisphosphatases and Thr/Ser/Cys in phosphoglycerate mutases., A number of sequence annotation errors in databases are highlighted by, this analysis. B. stearothermophilus PhoE is evolutionarily related to a, group of enzymes primarily present in Gram-positive bacilli. Even within, this group substrate specificity is clearly variable highlighting the, difficulties of computational functional annotation in the, cofactor-dependent phosphoglycerate mutase superfamily.
+
<StructureSection load='1h2f' size='340' side='right'caption='[[1h2f]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==About this Structure==
+
<table><tr><td colspan='2'>[[1h2f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H2F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H2F FirstGlance]. <br>
-
1H2F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with PO4 and VA3 as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: VA3. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H2F OCA].
+
</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=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=VA3:TRIVANADATE'>VA3</scene></td></tr>
-
==Reference==
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h2f OCA], [https://pdbe.org/1h2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h2f RCSB], [https://www.ebi.ac.uk/pdbsum/1h2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h2f ProSAT]</span></td></tr>
-
Structures of phosphate and trivanadate complexes of Bacillus stearothermophilus phosphatase PhoE: structural and functional analysis in the cofactor-dependent phosphoglycerate mutase superfamily., Rigden DJ, Littlejohn JE, Henderson K, Jedrzejas MJ, J Mol Biol. 2003 Jan 17;325(3):411-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12498792 12498792]
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/Q9ALU0_GEOSE Q9ALU0_GEOSE]
 +
== 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/h2/1h2f_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=1h2f ConSurf].
 +
<div style="clear:both"></div>
 +
__TOC__
 +
</StructureSection>
[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Jedrzejas, M.J.]]
+
[[Category: Jedrzejas MJ]]
-
[[Category: Littlejohn, J.]]
+
[[Category: Littlejohn JE]]
-
[[Category: Rigden, D.J.]]
+
[[Category: Rigden DJ]]
-
[[Category: PO4]]
+
-
[[Category: VA3]]
+
-
[[Category: broad specificity phosphatase; dpgm homolog]]
+
-
[[Category: hydrolase]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:26:31 2007''
+

Current revision

BACILLUS STEAROTHERMOPHILUS PHOE (previously known as yhfr) in complex with trivanadate

PDB ID 1h2f

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/1h2f"
Personal tools