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2V9M

L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT A87M- T109F-E192A)

Summary for 2V9M
Entry DOI10.2210/pdb2v9m/pdb
Related1GT7 1OJR 2UYU 2UYV 2V29 2V2A 2V2B 2V9E 2V9F 2V9G 2V9I 2V9L 2V9N 2V9O
DescriptorRHAMNULOSE-1-PHOSPHATE ALDOLASE, ZINC ION, CALCIUM ION, ... (6 entities in total)
Functional Keywordsentropy index, metal-binding, oligomerization, zinc, lyase, aldolase, class ii, cytoplasm, cleavage of l-rhamnulose-1-phosphate to dihydroxyacetoneph bacterial l-rhamnose metabolism, interface design, surface mutation, 2-ketose degradation, protein-protein interface, rare sugar, aggregation, zinc enzyme, fibrillation, rhamnose metabolism, protein engineering
Biological sourceESCHERICHIA COLI
Total number of polymer chains2
Total formula weight61435.50
Authors
Grueninger, D.,Schulz, G.E. (deposition date: 2007-08-24, release date: 2008-01-15, Last modification date: 2023-12-13)
Primary citationGrueninger, D.,Treiber, N.,Ziegler, M.O.P.,Koetter, J.W.A.,Schulze, M.-S.,Schulz, G.E.
Designed Protein-Protein Association.
Science, 319:206-, 2008
Cited by
PubMed Abstract: The analysis of natural contact interfaces between protein subunits and between proteins has disclosed some general rules governing their association. We have applied these rules to produce a number of novel assemblies, demonstrating that a given protein can be engineered to form contacts at various points of its surface. Symmetry plays an important role because it defines the multiplicity of a designed contact and therefore the number of required mutations. Some of the proteins needed only a single side-chain alteration in order to associate to a higher-order complex. The mobility of the buried side chains has to be taken into account. Four assemblies have been structurally elucidated. Comparisons between the designed contacts and the results will provide useful guidelines for the development of future architectures.
PubMed: 18187656
DOI: 10.1126/SCIENCE.1150421
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.3 Å)
Structure validation

227561

数据于2024-11-20公开中

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