4kxp: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4kxp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2f3h 2f3h]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KXP FirstGlance]. <br>
<table><tr><td colspan='2'>[[4kxp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2f3h 2f3h]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KXP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4kxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kxp OCA], [https://pdbe.org/4kxp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kxp RCSB], [https://www.ebi.ac.uk/pdbsum/4kxp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kxp ProSAT]</span></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=4kxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kxp OCA], [https://pdbe.org/4kxp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kxp RCSB], [https://www.ebi.ac.uk/pdbsum/4kxp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kxp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/F16P1_PIG F16P1_PIG]  
[https://www.uniprot.org/uniprot/F16P1_PIG F16P1_PIG]  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
AMP triggers a 15 degrees subunit-pair rotation in fructose-1,6-bisphosphatase (FBPase) from its active R-state to its inactive T-state. During this transition, a catalytically essential loop (residues 50-72) leaves its active (engaged) conformation. Structures of Ile10--&gt;Asp FBPase and molecular dynamic simulations here reveal factors responsible for loop displacement. AMP/Mg2+ and AMP/Zn2+ complexes of Asp10 FBPase are in intermediate quaternary conformations (completing 12 degrees of subunit-pair rotation), but the complex with Zn2+ provides the first instance of an engaged loop in a near-T quaternary state. The 12 degrees subunit-pair rotation generates close contacts involving the hinges (residues 50-57) and hairpin turns (residues 58-72) of the engaged loops. Additional subunit-pair rotation toward the T-state would make such contacts unfavorable, presumably causing displacement of the loop. Targeted molecular dynamics simulations reveal no steric barriers to subunit-pair rotations up to 14 degrees , followed by the displacement of the loop from the active site. Principal component analysis reveals high-amplitude motions that exacerbate steric clashes of engaged loops in the near-T state. The results of simulations and crystal structures are in agreement: subunit-pair rotations just short of the canonical T-state, coupled with high-amplitude modes, sterically displace the dynamic loop from the active site.
Mechanism of Displacement of a Catalytically Essential Loop from the Active Site of Mammalian Fructose-1,6-bisphosphatase.,Gao Y, Iancu CV, Mukund S, Choe JY, Honzatko RB Biochemistry. 2013 Jul 11. PMID:23844654<ref>PMID:23844654</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4kxp" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Fructose-1%2C6-bisphosphatase 3D structures|Fructose-1%2C6-bisphosphatase 3D structures]]
*[[Fructose-1%2C6-bisphosphatase 3D structures|Fructose-1%2C6-bisphosphatase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 15:16, 1 March 2024

Crystal Structure of AMP complexes of Porcine Liver Fructose-1,6-bisphosphatase Mutant I10D in T-stateCrystal Structure of AMP complexes of Porcine Liver Fructose-1,6-bisphosphatase Mutant I10D in T-state

Structural highlights

4kxp is a 2 chain structure with sequence from Sus scrofa. This structure supersedes the now removed PDB entry 2f3h. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

F16P1_PIG

See Also

4kxp, resolution 2.70Å

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