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1jtd

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(New page: 200px<br /><applet load="1jtd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jtd, resolution 2.30&Aring;" /> '''Crystal structure of...)
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[[Image:1jtd.gif|left|200px]]<br /><applet load="1jtd" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jtd.gif|left|200px]]<br /><applet load="1jtd" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jtd, resolution 2.30&Aring;" />
caption="1jtd, resolution 2.30&Aring;" />
'''Crystal structure of beta-lactamase inhibitor protein-II in complex with TEM-1 beta-lactamase'''<br />
'''Crystal structure of beta-lactamase inhibitor protein-II in complex with TEM-1 beta-lactamase'''<br />
==Overview==
==Overview==
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The structure of the 28 kDa beta-lactamase inhibitor protein-II (BLIP-II), in complex with the TEM-1 beta-lactamase has been determined to 2.3 A, resolution. BLIP-II is a secreted protein produced by the soil bacterium, Streptomyces exfoliatus SMF19 and is able to bind and inhibit TEM-1 with, subnanomolar affinity. BLIP-II is a seven-bladed beta-propeller with a, unique blade motif consisting of only three antiparallel beta-strands. The, overall fold is highly similar to the core structure of the human, regulator of chromosome condensation (RCC1). Although BLIP-II does not, share the same fold with BLIP, the first beta-lactamase inhibitor protein, for which structural data was available, a comparison of the two complexes, reveals a number of similarities and provides further insights into key, components of the TEM-1-BLIP and TEM-1-BLIP-II interfaces. Our preliminary, results from gene knock-out studies and scanning electron microscopy also, reveal a critical role of BLIP-II in sporulation.
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The structure of the 28 kDa beta-lactamase inhibitor protein-II (BLIP-II) in complex with the TEM-1 beta-lactamase has been determined to 2.3 A resolution. BLIP-II is a secreted protein produced by the soil bacterium Streptomyces exfoliatus SMF19 and is able to bind and inhibit TEM-1 with subnanomolar affinity. BLIP-II is a seven-bladed beta-propeller with a unique blade motif consisting of only three antiparallel beta-strands. The overall fold is highly similar to the core structure of the human regulator of chromosome condensation (RCC1). Although BLIP-II does not share the same fold with BLIP, the first beta-lactamase inhibitor protein for which structural data was available, a comparison of the two complexes reveals a number of similarities and provides further insights into key components of the TEM-1-BLIP and TEM-1-BLIP-II interfaces. Our preliminary results from gene knock-out studies and scanning electron microscopy also reveal a critical role of BLIP-II in sporulation.
==About this Structure==
==About this Structure==
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1JTD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Streptomyces_exfoliatus Streptomyces exfoliatus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JTD OCA].
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1JTD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Streptomyces_exfoliatus Streptomyces exfoliatus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JTD OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Streptomyces exfoliatus]]
[[Category: Streptomyces exfoliatus]]
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[[Category: Castro, L.De.]]
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[[Category: Castro, L De.]]
[[Category: Jensen, S.]]
[[Category: Jensen, S.]]
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[[Category: Kang, S.G.]]
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[[Category: Kang, S G.]]
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[[Category: Lee, H.S.]]
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[[Category: Lee, H S.]]
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[[Category: Lee, K.J.]]
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[[Category: Lee, K J.]]
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[[Category: Lim, D.C.]]
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[[Category: Lim, D C.]]
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[[Category: Park, H.U.]]
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[[Category: Park, H U.]]
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[[Category: Strynadka, N.C.J.]]
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[[Category: Strynadka, N C.J.]]
[[Category: CA]]
[[Category: CA]]
[[Category: beta-lactamase inhibitor protein-ii]]
[[Category: beta-lactamase inhibitor protein-ii]]
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[[Category: tem-1 beta-lactamase]]
[[Category: tem-1 beta-lactamase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:33:45 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:26:30 2008''

Revision as of 11:26, 21 February 2008


1jtd, resolution 2.30Å

Drag the structure with the mouse to rotate

Crystal structure of beta-lactamase inhibitor protein-II in complex with TEM-1 beta-lactamase

Overview

The structure of the 28 kDa beta-lactamase inhibitor protein-II (BLIP-II) in complex with the TEM-1 beta-lactamase has been determined to 2.3 A resolution. BLIP-II is a secreted protein produced by the soil bacterium Streptomyces exfoliatus SMF19 and is able to bind and inhibit TEM-1 with subnanomolar affinity. BLIP-II is a seven-bladed beta-propeller with a unique blade motif consisting of only three antiparallel beta-strands. The overall fold is highly similar to the core structure of the human regulator of chromosome condensation (RCC1). Although BLIP-II does not share the same fold with BLIP, the first beta-lactamase inhibitor protein for which structural data was available, a comparison of the two complexes reveals a number of similarities and provides further insights into key components of the TEM-1-BLIP and TEM-1-BLIP-II interfaces. Our preliminary results from gene knock-out studies and scanning electron microscopy also reveal a critical role of BLIP-II in sporulation.

About this Structure

1JTD is a Protein complex structure of sequences from Escherichia coli and Streptomyces exfoliatus with as ligand. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.

Reference

Crystal structure and kinetic analysis of beta-lactamase inhibitor protein-II in complex with TEM-1 beta-lactamase., Lim D, Park HU, De Castro L, Kang SG, Lee HS, Jensen S, Lee KJ, Strynadka NC, Nat Struct Biol. 2001 Oct;8(10):848-52. PMID:11573088

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