1jtd
From Proteopedia
(New page: 200px<br /><applet load="1jtd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jtd, resolution 2.30Å" /> '''Crystal structure of...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1jtd.gif|left|200px]]<br /><applet load="1jtd" size=" | + | [[Image:1jtd.gif|left|200px]]<br /><applet load="1jtd" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jtd, resolution 2.30Å" /> | caption="1jtd, resolution 2.30Å" /> | ||
'''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== | ||
| - | The structure of the 28 kDa beta-lactamase inhibitor protein-II (BLIP-II) | + | 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== | ||
| - | 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:// | + | 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== | ||
| Line 15: | Line 15: | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Streptomyces exfoliatus]] | [[Category: Streptomyces exfoliatus]] | ||
| - | [[Category: Castro, L | + | [[Category: Castro, L De.]] |
[[Category: Jensen, S.]] | [[Category: Jensen, S.]] | ||
| - | [[Category: Kang, S | + | [[Category: Kang, S G.]] |
| - | [[Category: Lee, H | + | [[Category: Lee, H S.]] |
| - | [[Category: Lee, K | + | [[Category: Lee, K J.]] |
| - | [[Category: Lim, D | + | [[Category: Lim, D C.]] |
| - | [[Category: Park, H | + | [[Category: Park, H U.]] |
| - | [[Category: Strynadka, N | + | [[Category: Strynadka, N C.J.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: beta-lactamase inhibitor protein-ii]] | [[Category: beta-lactamase inhibitor protein-ii]] | ||
| Line 29: | Line 29: | ||
[[Category: tem-1 beta-lactamase]] | [[Category: tem-1 beta-lactamase]] | ||
| - | ''Page seeded by [http:// | + | ''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
|
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
Page seeded by OCA on Thu Feb 21 13:26:30 2008
Categories: Beta-lactamase | Escherichia coli | Protein complex | Streptomyces exfoliatus | Castro, L De. | Jensen, S. | Kang, S G. | Lee, H S. | Lee, K J. | Lim, D C. | Park, H U. | Strynadka, N C.J. | CA | Beta-lactamase inhibitor protein-ii | Blip-ii | Protein-protein complex | Tem-1 beta-lactamase
