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| - | [[Image:1rdh.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1rdh| PDB=1rdh | SCENE= }} | | {{STRUCTURE_1rdh| PDB=1rdh | SCENE= }} |
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| - | '''CRYSTALLOGRAPHIC ANALYSES OF AN ACTIVE HIV-1 RIBONUCLEASE H DOMAIN SHOW STRUCTURAL FEATURES THAT DISTINGUISH IT FROM THE INACTIVE FORM'''
| + | ===CRYSTALLOGRAPHIC ANALYSES OF AN ACTIVE HIV-1 RIBONUCLEASE H DOMAIN SHOW STRUCTURAL FEATURES THAT DISTINGUISH IT FROM THE INACTIVE FORM=== |
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| - | ==Overview==
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| - | . An active recombinant preparation of the carboxy-terminal ribonuclease H (RNase H) domain of HIV-I reverse transcriptase has produced crystals of several different forms, including a trigonal prism form (P3(1); a = b = 52.03, c = 113.9 A with two molecules per asymmetric unit) and a hexagonal tablet form (P6(2)22 or P6(4)22; a = b = 93.5, c = 74.1 A with one molecule per asymmetric unit). The former appears to be isomorphous with crystals of a similar, but inactive, version of the enzyme that was used for a prior crystal structure determination [Davies, Hostomska, Hostomsky, Jordan & Matthews (1991). Science, 252, 88-95]. We have also obtained a structure solution for this crystal form and have refined it with 2.8 A resolution data (R = 0.216). We report here details of our crystallization studies and some initial structural results that verify that the preparation of active HIV-1 RNase H yields a protein that is not just enzymatically, but also structurally, distinguishable from the inactive form. Evidence suggests that region 538-542, which may be involved in the catalytic site and which is disordered in both molecules in the prior structure determination, is ordered in the crystal structure of the active enzyme, although the ordering may include more than one conformation for this loop. It should also be noted that, in the crystal structure of the trigonal form, RNase H monomers associate to form noncrystallographic twofold-symmetric dimers by fusing five-stranded mixed beta sheets into a single ten-stranded dimerwide sheet, an assembly that was not remarked upon by previous investigators.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15299518}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15299518 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15299518}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Einspahr, H M.]] | | [[Category: Einspahr, H M.]] |
| | [[Category: Finzel, B C.]] | | [[Category: Finzel, B C.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:21:46 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:50:52 2008'' |
Revision as of 17:50, 28 July 2008
Template:STRUCTURE 1rdh
CRYSTALLOGRAPHIC ANALYSES OF AN ACTIVE HIV-1 RIBONUCLEASE H DOMAIN SHOW STRUCTURAL FEATURES THAT DISTINGUISH IT FROM THE INACTIVE FORM
Template:ABSTRACT PUBMED 15299518
About this Structure
1RDH is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.
Reference
Crystallographic analyses of an active HIV-1 ribonuclease H domain show structural features that distinguish it from the inactive form., Chattopadhyay D, Finzel BC, Munson SH, Evans DB, Sharma SK, Strakalaitus NA, Brunner DP, Eckenrode FM, Dauter Z, Betzel C, Einspahr HM, Acta Crystallogr D Biol Crystallogr. 1993 Jul 1;49(Pt 4):423-7. PMID:15299518
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