1jtd: Difference between revisions

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[[Image:1jtd.gif|left|200px]]
{{Seed}}
[[Image:1jtd.png|left|200px]]


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{{STRUCTURE_1jtd|  PDB=1jtd  |  SCENE=  }}  
{{STRUCTURE_1jtd|  PDB=1jtd  |  SCENE=  }}  


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




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_11573088}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_11573088}}


==About this Structure==
==About this Structure==
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[[Category: Protein-protein complex]]
[[Category: Protein-protein complex]]
[[Category: Tem-1 beta-lactamase]]
[[Category: Tem-1 beta-lactamase]]
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