1gyn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:10, 13 December 2023) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1gyn.jpg|left|200px]]
 
-
{{Structure
+
==Class II fructose 1,6-bisphosphate aldolase with Cadmium (not Zinc) in the active site==
-
|PDB= 1gyn |SIZE=350|CAPTION= <scene name='initialview01'>1gyn</scene>, resolution 2.00&Aring;
+
<StructureSection load='1gyn' size='340' side='right'caption='[[1gyn]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=CD:CADMIUM ION'>CD</scene>
+
<table><tr><td colspan='2'>[[1gyn]] 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=1GYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GYN FirstGlance]. <br>
-
|ACTIVITY= [http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13]
+
</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>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</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=1gyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gyn OCA], [https://pdbe.org/1gyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gyn RCSB], [https://www.ebi.ac.uk/pdbsum/1gyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gyn ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ALF_ECOLI ALF_ECOLI] Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.<ref>PMID:10712619</ref>
 +
== 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/gy/1gyn_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=1gyn ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Previously determined crystal structures of the zinc enzyme Escherichia coli class II fructose-1,6-bisphosphate aldolase display good agreement for the protein structure but a differing metal-ion organization in the active site. The structure of the enzyme with Cd(2+) in place of Zn(2+) has now been determined to 2.0 A resolution to facilitate cation identification. The protein structure was essentially identical to other structures and five Cd(2+) positions were identified. Two of the cations are at the active site; one corresponds to the catalytic ion and the other provides a structural contribution. These Cd(2+) sites are equivalent to two Zn(2+) ions observed when the enzyme is complexed with a transition-state mimic and confirm our assignment of the roles played by these ions.
-
'''CLASS II FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE WITH CADMIUM (NOT ZINC) IN THE ACTIVE SITE'''
+
The organization of divalent cations in the active site of cadmium Escherichia coli fructose-1,6-bisphosphate aldolase.,Hall DR, Kemp LE, Leonard GA, Marshall K, Berry A, Hunter WN Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):611-4. Epub 2003, Feb 21. PMID:12595741<ref>PMID:12595741</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1gyn" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
Previously determined crystal structures of the zinc enzyme Escherichia coli class II fructose-1,6-bisphosphate aldolase display good agreement for the protein structure but a differing metal-ion organization in the active site. The structure of the enzyme with Cd(2+) in place of Zn(2+) has now been determined to 2.0 A resolution to facilitate cation identification. The protein structure was essentially identical to other structures and five Cd(2+) positions were identified. Two of the cations are at the active site; one corresponds to the catalytic ion and the other provides a structural contribution. These Cd(2+) sites are equivalent to two Zn(2+) ions observed when the enzyme is complexed with a transition-state mimic and confirm our assignment of the roles played by these ions.
+
*[[Aldolase 3D structures|Aldolase 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
1GYN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GYN OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
-
The organization of divalent cations in the active site of cadmium Escherichia coli fructose-1,6-bisphosphate aldolase., Hall DR, Kemp LE, Leonard GA, Marshall K, Berry A, Hunter WN, Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):611-4. Epub 2003, Feb 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12595741 12595741]
+
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Fructose-bisphosphate aldolase]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Berry A]]
-
[[Category: Berry, A.]]
+
[[Category: Hall DR]]
-
[[Category: Hall, D R.]]
+
[[Category: Hunter WN]]
-
[[Category: Hunter, W N.]]
+
[[Category: Kemp LE]]
-
[[Category: Kemp, L E.]]
+
[[Category: Leonard GA]]
-
[[Category: Leonard, G A.]]
+
-
[[Category: CD]]
+
-
[[Category: aldolase]]
+
-
[[Category: cadmium]]
+
-
[[Category: lyase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:29:46 2008''
+

Current revision

Class II fructose 1,6-bisphosphate aldolase with Cadmium (not Zinc) in the active site

PDB ID 1gyn

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/1gyn"
Personal tools