2f3b: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2f3b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F3B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2F3B FirstGlance]. <br> | <table><tr><td colspan='2'>[[2f3b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F3B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2F3B FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cnq|1cnq]], [[1eyi|1eyi]], [[1yxi|1yxi]], [[1yyz|1yyz]], [[1yzo|1yzo]], [[1q9d|1q9d]], [[2f3d|2f3d]], [[2f3h|2f3h]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cnq|1cnq]], [[1eyi|1eyi]], [[1yxi|1yxi]], [[1yyz|1yyz]], [[1yzo|1yzo]], [[1q9d|1q9d]], [[2f3d|2f3d]], [[2f3h|2f3h]]</td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FBP1,FBP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FBP1,FBP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG])</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f3b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f3b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2f3b RCSB], [http://www.ebi.ac.uk/pdbsum/2f3b PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f3b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f3b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2f3b RCSB], [http://www.ebi.ac.uk/pdbsum/2f3b PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Fructose-bisphosphatase]] | [[Category: Fructose-bisphosphatase]] | ||
[[Category: Pig]] | [[Category: Pig]] | ||
[[Category: Choe, J Y | [[Category: Choe, J Y]] | ||
[[Category: Fromm, H J | [[Category: Fromm, H J]] | ||
[[Category: Honzatko, R B | [[Category: Honzatko, R B]] | ||
[[Category: Iancu, C V | [[Category: Iancu, C V]] | ||
[[Category: Mukund, S | [[Category: Mukund, S]] | ||
[[Category: 6-bisphosphatase]] | [[Category: 6-bisphosphatase]] | ||
[[Category: Allosteric regulation]] | [[Category: Allosteric regulation]] | ||
Revision as of 19:26, 15 January 2015
Mechanism of displacement of a catalytically essential loop from the active site of fructose-1,6-bisphosphataseMechanism of displacement of a catalytically essential loop from the active site of fructose-1,6-bisphosphatase
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAMP 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-->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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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