1sat

From Proteopedia

(Difference between revisions)

Revision as of 02:52, 8 February 2016

CRYSTAL STRUCTURE OF THE 50 KDA METALLO PROTEASE FROM S. MARCESCENS

Structural highlights

1sat is a 1 chain structure with sequence from Serratia marcescens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[PRZN_SERMA] Has insecticidal activity against the locust M.palpalis. When administered orally to locusts at a low dose it causes them to lie on their sides exhibiting sporadic limb movements and muscular twitching, followed by full recovery. When administered at higher doses the same symptoms are observed, followed by death.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystal structure of the 50 kDa metalloprotease from the Gram-negative bacterium Serratia marcescens has been solved and refined to a crystallographic R-factor of 0.192 at 1.80 A resolution. The structure is very similar to that of alkaline protease from Pseudomonas aeruginosa, in particular the calcium binding "parallel beta roll" motif is completely conserved. The N-terminal proteolytic domain shows the typical "metzincin" fold. The active sites of the two enzymes are slightly different, Tyr216 is a Zn ligand in the Serratia metallo protease. The loops 70-77 and 122-132, which encompass the active site cleft, differ due to insertions and deletions so that the Serratia metallo protease seems to have a more open site than the alkaline protease.

Crystal structure of the 50 kDa metallo protease from Serratia marcescens.,Baumann U J Mol Biol. 1994 Sep 23;242(3):244-51. PMID:8089845^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Baumann U. Crystal structure of the 50 kDa metallo protease from Serratia marcescens. J Mol Biol. 1994 Sep 23;242(3):244-51. PMID:8089845 doi:http://dx.doi.org/10.1006/jmbi.1994.1576

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1sat"

Categories: Serratia marcescens | Baumann, U | Parallel beta helix | Parallel beta roll

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     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1sat ConSurf].
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1sat

From Proteopedia

Revision as of 02:52, 8 February 2016

CRYSTAL STRUCTURE OF THE 50 KDA METALLO PROTEASE FROM S. MARCESCENS

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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