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7W12

Complex structure of alginate lyase AlyB-OU02 with G9

Summary for 7W12
Entry DOI10.2210/pdb7w12/pdb
DescriptorAlginate lyase, alpha-L-gulopyranuronic acid-(1-4)-alpha-L-gulopyranuronic acid-(1-4)-alpha-L-gulopyranuronic acid-(1-4)-alpha-L-gulopyranuronic acid-(1-4)-alpha-L-gulopyranuronic acid-(1-4)-alpha-L-gulopyranuronic acid-(1-4)-alpha-L-gulopyranuronic acid-(1-4)-alpha-L-gulopyranuronic acid-(1-4)-alpha-L-gulopyranuronic acid, SULFATE ION, ... (4 entities in total)
Functional Keywordspl7 family, alginate lyase, complex, lyase
Biological sourceVibrio splendidus
Total number of polymer chains1
Total formula weight55817.70
Authors
Liu, W.Z.,Lyu, Q.Q.,Zhang, K.K. (deposition date: 2021-11-19, release date: 2022-11-16, Last modification date: 2024-10-09)
Primary citationZhang, K.,Li, Z.,Zhu, Q.,Cao, H.,He, X.,Zhang, X.H.,Liu, W.,Lyu, Q.
Determination of oligosaccharide product distributions of PL7 alginate lyases by their structural elements.
Commun Biol, 5:782-782, 2022
Cited by
PubMed Abstract: Alginate lyases can be used to produce well-defined alginate oligosaccharides (AOSs) because of their specificities for AOS products. A large number of alginate lyases have been recorded in the CAZy database; however, the majority are annotated-only alginate lyases that include little information on their products, thus limiting their applications. Here, we establish a simple and experiment-saving approach to predict product distributions for PL7 alginate lyases through extensive structural biology, bioinformatics and biochemical studies. Structural study on several PL7 alginate lyases reveals that two loops around the substrate binding cleft determine product distribution. Furthermore, a database containing the loop information of all annotated-only single-domain PL7 alginate lyases is constructed, enabling systematic exploration of the association between loop and product distribution. Based on these results, a simplified loop/product distribution relationship is proposed, giving us information on product distribution directly from the amino acid sequence.
PubMed: 35918517
DOI: 10.1038/s42003-022-03721-1
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.25 Å)
Structure validation

226707

數據於2024-10-30公開中

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