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1k6y

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(New page: 200px<br /> <applet load="1k6y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k6y, resolution 2.4&Aring;" /> '''Crystal Structure of...)
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<applet load="1k6y" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Crystal Structure of a Two-Domain Fragment of HIV-1 Integrase'''<br />
'''Crystal Structure of a Two-Domain Fragment of HIV-1 Integrase'''<br />
==Overview==
==Overview==
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Retroviral integrase, an essential enzyme for replication of human, immunodeficiency virus type-1 (HIV-1) and other retroviruses, contains, three structurally distinct domains, an N-terminal domain, the catalytic, core and a C-terminal domain. To elucidate their spatial arrangement, we, have solved the structure of a fragment of HIV-1 integrase comprising the, N-terminal and catalytic core domains. This structure reveals a dimer, interface between the N-terminal domains different from that observed for, the isolated domain. It also complements the previously determined, structure of the C-terminal two domains of HIV-1 integrase; superposition, of the conserved catalytic core of the two structures results in a, plausible full-length integrase dimer. Furthermore, an integrase tetramer, formed by crystal lattice contacts bears structural resemblance to a, related bacterial transposase, Tn5, and exhibits positively charged, channels suitable for DNA binding.
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Retroviral integrase, an essential enzyme for replication of human immunodeficiency virus type-1 (HIV-1) and other retroviruses, contains three structurally distinct domains, an N-terminal domain, the catalytic core and a C-terminal domain. To elucidate their spatial arrangement, we have solved the structure of a fragment of HIV-1 integrase comprising the N-terminal and catalytic core domains. This structure reveals a dimer interface between the N-terminal domains different from that observed for the isolated domain. It also complements the previously determined structure of the C-terminal two domains of HIV-1 integrase; superposition of the conserved catalytic core of the two structures results in a plausible full-length integrase dimer. Furthermore, an integrase tetramer formed by crystal lattice contacts bears structural resemblance to a related bacterial transposase, Tn5, and exhibits positively charged channels suitable for DNA binding.
==About this Structure==
==About this Structure==
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1K6Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] with ZN, K and PO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/RNA-directed_DNA_polymerase RNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.49 2.7.7.49] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K6Y OCA].
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1K6Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=K:'>K</scene> and <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/RNA-directed_DNA_polymerase RNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.49 2.7.7.49] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K6Y OCA].
==Reference==
==Reference==
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[[Category: integrase]]
[[Category: integrase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 14:15:28 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:30:48 2008''

Revision as of 11:30, 21 February 2008


1k6y, resolution 2.4Å

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Crystal Structure of a Two-Domain Fragment of HIV-1 Integrase

Overview

Retroviral integrase, an essential enzyme for replication of human immunodeficiency virus type-1 (HIV-1) and other retroviruses, contains three structurally distinct domains, an N-terminal domain, the catalytic core and a C-terminal domain. To elucidate their spatial arrangement, we have solved the structure of a fragment of HIV-1 integrase comprising the N-terminal and catalytic core domains. This structure reveals a dimer interface between the N-terminal domains different from that observed for the isolated domain. It also complements the previously determined structure of the C-terminal two domains of HIV-1 integrase; superposition of the conserved catalytic core of the two structures results in a plausible full-length integrase dimer. Furthermore, an integrase tetramer formed by crystal lattice contacts bears structural resemblance to a related bacterial transposase, Tn5, and exhibits positively charged channels suitable for DNA binding.

About this Structure

1K6Y is a Single protein structure of sequence from Human immunodeficiency virus 1 with , and as ligands. Active as RNA-directed DNA polymerase, with EC number 2.7.7.49 Full crystallographic information is available from OCA.

Reference

Structure of a two-domain fragment of HIV-1 integrase: implications for domain organization in the intact protein., Wang JY, Ling H, Yang W, Craigie R, EMBO J. 2001 Dec 17;20(24):7333-43. PMID:11743009

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