1dzz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:17, 9 April 2025) (edit) (undo)
 
(21 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1dzz.gif|left|200px]]<br />
 
-
<applet load="1dzz" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1dzz, resolution 1.92&Aring;" />
 
-
'''L-FUCULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI MUTANT Y113F'''<br />
 
-
==Overview==
+
==L-Fuculose-1-Phosphate Aldolase from Escherichia coli Mutant Y113F==
-
Previous analyses established the structures of unligated L-fuculose, 1-phosphate aldolase and of the enzyme ligated with an inhibitor mimicking, the substrate dihydroxyacetone phosphate. These data allowed us to suggest, a catalytic mechanism. On the basis of this proposal, numerous mutations, were now introduced at the active center and tested with respect to their, catalytic rates and their product distributions. For several mutants, the, structures were determined. The results demonstrate the catalytic, importance of some particular residues in defined conformations and in the, mobile C-terminal chain end. Moreover, they led to a modification of the, proposed mechanism. The effect of some mutations on enantioselectivity and, on the ratio of diastereomer formation indicates clearly the ... [[http://ispc.weizmann.ac.il/pmbin/getpm?10821675 (full description)]]
+
<StructureSection load='1dzz' size='340' side='right'caption='[[1dzz]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1dzz]] is a 1 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=1DZZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DZZ 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]] 1.92&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1dzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dzz OCA], [https://pdbe.org/1dzz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dzz RCSB], [https://www.ebi.ac.uk/pdbsum/1dzz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dzz ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/FUCA_ECOLI FUCA_ECOLI]
 +
== 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/dz/1dzz_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1dzz ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Previous analyses established the structures of unligated L-fuculose 1-phosphate aldolase and of the enzyme ligated with an inhibitor mimicking the substrate dihydroxyacetone phosphate. These data allowed us to suggest a catalytic mechanism. On the basis of this proposal, numerous mutations were now introduced at the active center and tested with respect to their catalytic rates and their product distributions. For several mutants, the structures were determined. The results demonstrate the catalytic importance of some particular residues in defined conformations and in the mobile C-terminal chain end. Moreover, they led to a modification of the proposed mechanism. The effect of some mutations on enantioselectivity and on the ratio of diastereomer formation indicates clearly the binding site of the aldehyde moiety in relation to the other substrate dihydroxyacetone phosphate.
-
==About this Structure==
+
Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis.,Joerger AC, Gosse C, Fessner WD, Schulz GE Biochemistry. 2000 May 23;39(20):6033-41. PMID:10821675<ref>PMID:10821675</ref>
-
1DZZ 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 ZN, SO4 and BME as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/L-fuculose-phosphate_aldolase L-fuculose-phosphate aldolase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.17 4.1.2.17]]. Structure known Active Sites: ACT, MUT and PBS. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DZZ OCA]].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Catalytic action of fuculose 1-phosphate aldolase (class II) as derived from structure-directed mutagenesis., Joerger AC, Gosse C, Fessner WD, Schulz GE, Biochemistry. 2000 May 23;39(20):6033-41. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10821675 10821675]
+
</div>
-
[[Category: Escherichia coli]]
+
<div class="pdbe-citations 1dzz" style="background-color:#fffaf0;"></div>
-
[[Category: L-fuculose-phosphate aldolase]]
+
-
[[Category: Single protein]]
+
-
[[Category: Joerger, A.C.]]
+
-
[[Category: Schulz, G.E.]]
+
-
[[Category: BME]]
+
-
[[Category: SO4]]
+
-
[[Category: ZN]]
+
-
[[Category: aldolase (class ii)]]
+
-
[[Category: bacterial l-fucose metabolism]]
+
-
[[Category: cleavage of l-fuculose-1-phosphate to dihydroxyacetonephosphate and l-lactaldehyde]]
+
-
[[Category: mutant structure]]
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:03:28 2007''
+
==See Also==
 +
*[[Aldolase 3D structures|Aldolase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Escherichia coli]]
 +
[[Category: Large Structures]]
 +
[[Category: Joerger AC]]
 +
[[Category: Schulz GE]]

Current revision

L-Fuculose-1-Phosphate Aldolase from Escherichia coli Mutant Y113F

PDB ID 1dzz

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/1dzz"
Personal tools