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1a49

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[[Image:1a49.gif|left|200px]]
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[[Image:1a49.png|left|200px]]
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{{STRUCTURE_1a49| PDB=1a49 | SCENE= }}
{{STRUCTURE_1a49| PDB=1a49 | SCENE= }}
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'''BIS MG-ATP-K-OXALATE COMPLEX OF PYRUVATE KINASE'''
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===BIS MG-ATP-K-OXALATE COMPLEX OF PYRUVATE KINASE===
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==Overview==
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Pyruvate kinase from rabbit muscle has been cocrystallized as a complex with MgIIATP, oxalate, Mg2+, and either K+ or Na+. Crystals with either Na+ or K+ belong to the space group P2(1)2(1)2(1), and the asymmetric units contain two tetramers. The structures were solved by molecular replacement and refined to 2.1 (K+) and 2.35 A (Na+) resolution. The structures of the Na+ and K+ complexes are virtually isomorphous. Each of the eight subunits within the asymmetric unit contains MgIIoxalate as a bidentate complex linked to the protein through coordination of Mg2+ to the carboxylates of Glu 271 and Asp 295. Six of the subunits also contain an alpha,beta,gamma-tridentate complex of MgIIATP, and the active-site cleft, located between domains A and B, is closed in these subunits. In the remaining two subunits MgIIATP is missing, and the active-site cleft is open. Closure of the active-site cleft in the fully liganded subunits includes a rotation of 41 degrees of the B domain relative to the A domain. alpha-Carbons of residues in the B domain undergo movements of up to 17.8 A (Lys 124) in the cleft closure. Lys 206, Arg 119, and Asp 177 from the B domain move several angstroms from their positions in the open conformation to contact the MgIIATP complex in the active site. The gamma-phosphate of ATP coordinates to both magnesium ions and to the monovalent cation, K+ or Na+. A Mg2+-coordinated oxygen from the MgIIoxalate complex lies 3.0 A from Pgamma of ATP, and this oxygen is positioned for an in-line attack on the phosphorus. The side chains of Lys 269 and Arg 119 are positioned to provide leaving-group activation in the forward and reverse directions. There is no obvious candidate for the acid/base catalyst near the 2-si face of the prospective enolate of the normal substrate. A functional group linked through solvent and side-chain hydroxyls may function in a proton relay.
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The line below this paragraph, {{ABSTRACT_PUBMED_9572839}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 9572839 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9572839}}
==About this Structure==
==About this Structure==
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[[Category: Rabbit muscle]]
[[Category: Rabbit muscle]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:47:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:03:38 2008''

Revision as of 13:04, 30 June 2008

Image:1a49.png

Template:STRUCTURE 1a49

BIS MG-ATP-K-OXALATE COMPLEX OF PYRUVATE KINASE

Template:ABSTRACT PUBMED 9572839

About this Structure

1A49 is a Single protein structure of sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

Structure of the bis(Mg2+)-ATP-oxalate complex of the rabbit muscle pyruvate kinase at 2.1 A resolution: ATP binding over a barrel., Larsen TM, Benning MM, Rayment I, Reed GH, Biochemistry. 1998 May 5;37(18):6247-55. PMID:9572839

Page seeded by OCA on Mon Jun 30 16:03:38 2008

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