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1gq8
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Pectin is a principal component in the primary cell wall of plants. During | + | Pectin is a principal component in the primary cell wall of plants. During cell development, pectin is modified by pectin methylesterases to give different properties to the cell wall. This report describes the first crystal structure of a plant pectin methylesterase. The beta-helical structure embodies a central cleft, lined by several aromatic residues, that has been deduced to be suitable for pectin binding. The active site is found at the center of this cleft where Asp157 is suggested to act as the nucleophile, Asp136 as an acid/base and Gln113/Gln135 to form an anion hole to stabilize the transition state. |
==About this Structure== | ==About this Structure== | ||
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[[Category: pectin methylesterase]] | [[Category: pectin methylesterase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:52:48 2008'' |
Revision as of 10:52, 21 February 2008
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PECTIN METHYLESTERASE FROM CARROT
Overview
Pectin is a principal component in the primary cell wall of plants. During cell development, pectin is modified by pectin methylesterases to give different properties to the cell wall. This report describes the first crystal structure of a plant pectin methylesterase. The beta-helical structure embodies a central cleft, lined by several aromatic residues, that has been deduced to be suitable for pectin binding. The active site is found at the center of this cleft where Asp157 is suggested to act as the nucleophile, Asp136 as an acid/base and Gln113/Gln135 to form an anion hole to stabilize the transition state.
About this Structure
1GQ8 is a Single protein structure of sequence from Daucus carota with as ligand. Active as Pectinesterase, with EC number 3.1.1.11 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure of plant pectin methylesterase., Johansson K, El-Ahmad M, Friemann R, Jornvall H, Markovic O, Eklund H, FEBS Lett. 2002 Mar 13;514(2-3):243-9. PMID:11943159
Page seeded by OCA on Thu Feb 21 12:52:48 2008
