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2OKH

Crystal structure of dimeric form of PfFabZ in crystal form3

Summary for 2OKH
Entry DOI10.2210/pdb2okh/pdb
Related1U1Z 1Z6B 1ZHG 2OKI
DescriptorBeta-hydroxyacyl-ACP dehydratase (2 entities in total)
Functional Keywordsfabz, hotdog fold, non-isomorphism, plasmodium, lyase
Biological sourcePlasmodium falciparum (malaria parasite P. falciparum)
Total number of polymer chains2
Total formula weight29981.30
Authors
Swarnamukhi, P.L.,Sharma, S.K.,Padala, P.,Surolia, N.,Surolia, A.,Suguna, K. (deposition date: 2007-01-16, release date: 2007-04-10, Last modification date: 2023-10-25)
Primary citationSwarnamukhi, P.L.,Sharma, S.K.,Padala, P.,Surolia, N.,Surolia, A.,Suguna, K.
Packing and loop-structure variations in non-isomorphous crystals of FabZ from Plasmodium falciparum
ACTA CRYSTALLOGR.,SECT.D, 63:458-464, 2007
Cited by
PubMed Abstract: The crystals obtained from various batches of crystallization trials of FabZ from Plasmodium falciparum exhibited non-isomorphism. The c axis of the I222 cell showed a large variation of about 16 A, from c = 81 A to c = 97 A. Complete data sets were collected for three crystal forms with varying lengths of the c axis (form 1, c = 97 A; form 2, c = 92 A; form 3, c = 81 A). The crystal structure of form 1 has been reported previously. Here, the crystal structures of the other two crystal forms are reported and a detailed structural comparison is made of the three crystal forms in order to explore the possible reasons for the existence of non-isomorphism. The conformations of three loops vary between the three crystal forms. The disposition of the loops affects the crystal packing and hence the unit-cell parameter. The crystallization condition and crystallization method employed, which change the evaporation rate, determine the crystal form of the enzyme. The present analysis shows that pH-induced intrinsic conformational changes in the protein play a key role in the observed differences.
PubMed: 17372349
DOI: 10.1107/S0907444907003228
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

237735

數據於2025-06-18公開中

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