2oki

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(New page: 200px<br /><applet load="2oki" size="350" color="white" frame="true" align="right" spinBox="true" caption="2oki, resolution 2.70&Aring;" /> '''Crystal structure of...)
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==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Padala, P.]]
[[Category: Padala, P.]]
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[[Category: Sharma, S.K.]]
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[[Category: Sharma, S K.]]
[[Category: Suguna, K.]]
[[Category: Suguna, K.]]
[[Category: Surolia, A.]]
[[Category: Surolia, A.]]
[[Category: Surolia, N.]]
[[Category: Surolia, N.]]
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[[Category: Swarnamukhi, P.L.]]
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[[Category: Swarnamukhi, P L.]]
[[Category: fabz]]
[[Category: fabz]]
[[Category: hotdog fold]]
[[Category: hotdog fold]]
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[[Category: plasmodium]]
[[Category: plasmodium]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 21:12:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:19:33 2008''

Revision as of 16:19, 21 February 2008


2oki, resolution 2.70Å

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Crystal structure of dimeric form of PfFabZ in crystal form2

Overview

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.

About this Structure

2OKI is a Single protein structure of sequence from Plasmodium falciparum. Active as [acyl-carrier-protein_dehydratase 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase], with EC number 4.2.1.60 Full crystallographic information is available from OCA.

Reference

Packing and loop-structure variations in non-isomorphous crystals of FabZ from Plasmodium falciparum., Swarnamukhi PL, Sharma SK, Padala P, Surolia N, Surolia A, Suguna K, Acta Crystallogr D Biol Crystallogr. 2007 Apr;63(Pt 4):458-64. Epub 2007, Mar 16. PMID:17372349 [[Category: 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase]]

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