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1lxt
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Data between 6.0 and 2.4 A resolution, collected at 253 K, wer used to, refine a revised atomic model of muscle phosphoglucomutase: final, crystallographic R factor = 16.3% (Rfree = 19.1%); final r.m.s. deviations, from ideal bond lengths and angles = 0.018 A and 3.2 degrees, respectively. Features of the protein that were recognized only in the, revised model include: the disposition of water molecules within, domain-domain interfaces; two ion pairs buried in domain-domain, interfaces, one of which is a structural arginine around which the, active-site phosphoserine loop is wound; the basic architecture of the, active-site 'crevice', which is a groove in a 1(1/3)-turn helix, open at, both ends, that is produced by the interfacing of the four domains; the, distorted hexacoordinate ligand | + | Data between 6.0 and 2.4 A resolution, collected at 253 K, wer used to, refine a revised atomic model of muscle phosphoglucomutase: final, crystallographic R factor = 16.3% (Rfree = 19.1%); final r.m.s. deviations, from ideal bond lengths and angles = 0.018 A and 3.2 degrees, respectively. Features of the protein that were recognized only in the, revised model include: the disposition of water molecules within, domain-domain interfaces; two ion pairs buried in domain-domain, interfaces, one of which is a structural arginine around which the, active-site phosphoserine loop is wound; the basic architecture of the, active-site 'crevice', which is a groove in a 1(1/3)-turn helix, open at, both ends, that is produced by the interfacing of the four domains; the, distorted hexacoordinate ligand sphere of the active-site Mg2+, where the, enzymic phosphate group acts as a bidentate ligand; a pair of arginine, residues in domain IV that form part of the enzymic phosphate-binding site, (distal subsite) whose disposition in the two monomers of the asymmetric, unit is affected unequally by distant crystallographic contacts;, structural differences throughout domain IV, produced by these differing, contacts, that may mimic solution differences induced by substrate, binding; large differences in individually refined Debye-Waller thermal, factors for corresponding main-chain atoms in monomers (1) and (2), suggesting a dynamic disorder within the crystal that may involve, domain-size groups of residues; and a 'nucleophilic elbow' in the active, site that resides in a topological environment differing from previous, descriptions of this type of structure in other proteins. |
==About this Structure== | ==About this Structure== | ||
| - | 1LXT is a | + | 1LXT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with CD and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoglucomutase Phosphoglucomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.2 5.4.2.2] Structure known Active Sites: MBA and MBB. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LXT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: phosphotransferase]] | [[Category: phosphotransferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:14:18 2007'' |
Revision as of 11:08, 5 November 2007
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STRUCTURE OF PHOSPHOTRANSFERASE PHOSPHOGLUCOMUTASE FROM RABBIT
Overview
Data between 6.0 and 2.4 A resolution, collected at 253 K, wer used to, refine a revised atomic model of muscle phosphoglucomutase: final, crystallographic R factor = 16.3% (Rfree = 19.1%); final r.m.s. deviations, from ideal bond lengths and angles = 0.018 A and 3.2 degrees, respectively. Features of the protein that were recognized only in the, revised model include: the disposition of water molecules within, domain-domain interfaces; two ion pairs buried in domain-domain, interfaces, one of which is a structural arginine around which the, active-site phosphoserine loop is wound; the basic architecture of the, active-site 'crevice', which is a groove in a 1(1/3)-turn helix, open at, both ends, that is produced by the interfacing of the four domains; the, distorted hexacoordinate ligand sphere of the active-site Mg2+, where the, enzymic phosphate group acts as a bidentate ligand; a pair of arginine, residues in domain IV that form part of the enzymic phosphate-binding site, (distal subsite) whose disposition in the two monomers of the asymmetric, unit is affected unequally by distant crystallographic contacts;, structural differences throughout domain IV, produced by these differing, contacts, that may mimic solution differences induced by substrate, binding; large differences in individually refined Debye-Waller thermal, factors for corresponding main-chain atoms in monomers (1) and (2), suggesting a dynamic disorder within the crystal that may involve, domain-size groups of residues; and a 'nucleophilic elbow' in the active, site that resides in a topological environment differing from previous, descriptions of this type of structure in other proteins.
About this Structure
1LXT is a Single protein structure of sequence from Oryctolagus cuniculus with CD and SO4 as ligands. Active as Phosphoglucomutase, with EC number 5.4.2.2 Structure known Active Sites: MBA and MBB. Full crystallographic information is available from OCA.
Reference
Structure of rabbit muscle phosphoglucomutase refined at 2.4 A resolution., Liu Y, Ray WJ Jr, Baranidharan S, Acta Crystallogr D Biol Crystallogr. 1997 Jul 1;53(Pt 4):392-405. PMID:15299905
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